US6077824A - Methods for improving the activity of δ-endotoxins against insect pests - Google Patents
Methods for improving the activity of δ-endotoxins against insect pests Download PDFInfo
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- C07K14/195—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from bacteria
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- C07K14/325—Bacillus thuringiensis crystal protein (delta-endotoxin)
Abstract
Disclosed are methods for increasing the activity of B. thuringiensis delta -endotoxins against Coleopteran insect pests. Also disclosed are methods for mutagenizing nucleic acid sequences encoding these polypeptides, and increasing insect resistance in transgenic plants expressing these genes.
Description
1.1 Field of the Invention
This invention relates to methods for producing genetically-engineered, recombinant δ-endotoxins derived from Bacillus thuringiensis that are useful in the control of southern corn rootworm (Diabrotica undecimpunctata howardi Barber) and western corn rootworm (Diabrotica virgifera virgifera LeConte).
1.2 Description of the Related Art
Almost all field crops, plants, and commercial farming areas are susceptible to attack by one or more insect pests. Particularly problematic are Coleopteran and Lepidoptern pests. For example, vegetable and cole crops such as artichokes, kohlrabi, arugula, leeks, asparagus, lentils, beans, lettuce (e.g., head, leaf, romaine), beets, bok choy, malanga, broccoli, melons (e.g., muskmelon, watermelon, crenshaw, honeydew, cantaloupe), brussels sprouts, cabbage, cardoni, carrots, napa, cauliflower, okra, onions, celery, parsley, chick peas, parsnips, chicory, peas, chinese cabbage, peppers, collards, potatoes, cucumber, pumpkins, cucurbits, radishes, dry bulb onions, rutabaga, eggplant, salsify, escarole, shallots, endive, soybean, garlic, spinach, green onions, squash, greens, sugar beets, sweet potatoes, turnip, swiss chard, horseradish, tomatoes, kale, turnips, and a variety of spices are sensitive to infestation by one or more of the following insect pests: alfalfa looper, armyworm, beet armyworm, artichoke plume moth, cabbage budworm, cabbage looper, cabbage webworm, corn earworm, celery leafeater, cross-striped cabbageworm, european corn borer, diamondback moth, green cloverworm, imported cabbageworm, melonworm, omnivorous leafroller, pickleworm, rindworm complex, saltmarsh caterpillar, soybean looper, tobacco budworm, tomato fruitworm, tomato hornworm, tomato pinworm, velvetbean caterpillar, and yellowstriped armyworm. Likewise, pasture and hay crops such as alfalfa, pasture grasses and silage are often attacked by such pests as armyworm, beef armyworm, alfalfa caterpillar, European skipper, a variety of loopers and webworms, as well as yellowstriped armyworms.
Fruit and vine crops such as apples, apricots, cherries, nectarines, peaches, pears, plums, prunes, quince almonds, chestnuts, filberts, pecans, pistachios, walnuts, citrus, blackberries, blueberries, boysenberries, cranberries, currants, loganberries, raspberries, strawberries, grapes, avocados, bananas, kiwi, persimmons, pomegranate, pineapple, tropical fruits are often susceptible to attack and defoliation by achema sphinx moth, amorbia, armyworm, citrus cutworm, banana skipper, blackheaded fireworm, blueberry leafroller, cankerworm, cherry fruitworm, citrus cutworm, cranberry girdler, eastern tent caterpillar, fall webworm, fall webworm, filbert leafroller, filbert webworm, fruit tree leafroller, grape berry moth, grape leaffolder, grapeleaf skeletonizer, green fruitworm, gummosos-batrachedra commosae, gypsy moth, hickory shuckworm, hornworms, loopers, navel orangeworm, obliquebanded leafroller, omnivorous leafroller, omnivorous looper, orange tortrix, orangedog, oriental fruit moth, pandemis leafroller, peach twig borer, pecan nut casebearer, redbanded leafroller, redhumped caterpillar, roughskinned cutworm, saltmarsh caterpillar, spanworm, tent caterpillar, thecla-thecla basillides, tobacco budworm, tortrix moth, tufted apple budmoth, variegated leafroller, walnut caterpillar, western tent caterpillar, and yellowstriped armyworm.
Field crops such as canola/rape seed, evening primrose, meadow foam, corn (field, sweet, popcorn), cotton, hops, jojoba, peanuts, rice, safflower, small grains (barley, oats, rye, wheat, etc.), sorghum, soybeans, sunflowers, and tobacco are often targets for infestation by insects including armyworm, asian and other corn borers, banded sunflower moth, beet armyworm, bollworm, cabbage looper, corn rootworm (including southern and western varieties), cotton leaf perforator, diamondback moth, european corn borer, green cloverworm, headmoth, headworm, imported cabbageworm, loopers (including Anacamptodes spp.), obliquebanded leafroller, omnivorous leaftier, podworm, podworm, saltmarsh caterpillar, southwestern corn borer, soybean looper, spotted cutworm, sunflower moth, tobacco budworm, tobacco hornworm, velvetbean caterpillar,
Bedding plants, flowers, ornamentals, vegetables and container stock are frequently fed upon by a host of insect pests such as armyworm, azalea moth, beet armyworm, diamondback moth, ello moth (hornworm), Florida fern caterpillar, Io moth, loopers, oleander moth, omnivorous leafroller, omnivorous looper, and tobacco budworm.
Forests, fruit, ornamental, and nut-bearing trees, as well as shrubs and other nursery stock are often susceptible to attack from diverse insects such as bagworm, blackheaded budworm, browntail moth, california oakworm, douglas fir tussock moth, elm spanworm, fall webwormn, fruittree leafroller, greenstriped mapleworm, gypsy moth, jack pine budworm, mimosa webworm, pine butterfly, redhumped caterpillar, saddleback caterpillar, saddle prominent caterpillar, spring and fall cankerworm, spruce budworm, tent caterpillar, tortrix, and western tussock moth. Likewise, turf grasses are often attacked by pests such as armyworm, sod webworm, and tropical sod webworm.
Because crops of commercial interest are often the target of insect attack, environmentally-sensitive methods for controlling or eradicating insect infestation are desirable in many instances. This is particularly true for farmers, nurserymen, growers, and commercial and residential areas which seek to control insect populations using eco-friendly compositions.
The most widely used environmentally-sensitive insecticidal formulations developed in recent years have been composed of microbial pesticides derived from the bacterium Bacillus thuringiensis. B. thuringiensis is a Gram-positive bacterium that produces crystal proteins or inclusion bodies which are specifically toxic to certain orders and species of insects. Many different strains of B. thuringiensis have been shown to produce insecticidal crystal proteins. Compositions including B. thuringiensis strains which produce insecticidal proteins have been commercially-available and used as environmentally-acceptable insecticides because they are quite toxic to the specific target insect, but are harmless to plants and other non-targeted organisms.
δ-endotoxins are used to control a wide range of leaf-eating caterpillars and beetles, as well as mosquitoes. These proteinaceous parasporal crystals, also referred to as insecticidal crystal proteins, crystal proteins, Bt inclusions, crystaline inclusions, inclusion bodies, and Bt toxins, are a large collection of insecticidal proteins produced by B. thuringiensis that are toxic upon ingestion by a susceptible insect host. Over the past decade research on the structure and function of B. thuringiensis toxins has covered all of the major toxin categories, and while these toxins differ in specific structure and function, general similarities in the structure and function are assumed. Based on the accumulated knowledge of B. thuringiensis toxins, a generalized mode of action for B. thuringiensis toxins has been created and includes: ingestion by the insect, solubilization in the insect midgut (a combination stomach and small intestine), resistance to digestive enzymes sometimes with partial digestion actually "activating" the toxin, binding to the midgut cells, formation of a pore in the insect cells and the disruption of cellular homeostasis (English and Slatin, 1992).
Many of the δ-endotoxins are related to various degrees by similarities in their amino acid sequences. Historically, the proteins and the genes which encode them were classified based largely upon their spectrum of insecticidal activity. The review by Hofte and Whiteley (1989) discusses the genes and proteins that were identified in B. thuringiensis prior to 1990, and sets forth the nomenclature and classification scheme which has traditionally been applied to B. thuringiensis genes and proteins. cryI genes encode lepidopterantoxic cryI proteins. cryII genes encode cryII proteins that are toxic to both lepidopterans and dipterans. cryIII genes encode coleopteran-toxic CryIII proteins, while cryIV genes encode dipteran-toxic CryIV proteins.
Based on the degree of sequence similarity, the proteins were further classified into subfamilies; more highly related proteins within each family were assigned divisional letters such as CryIA, cryIB, CryIC, etc. Even more closely related proteins within each division were given names such as CryIC1, CryIC2, etc.
Recently a new nomenclature was developed which systematically classified the Cry proteins based upon amino acid sequence homology rather than upon insect target specificities. The classification scheme for many known toxins, not including allelic variations in individual proteins, is summarized in Table 1.
TABLE 1 ______________________________________ KNOWN B. THURINGIENSIS δ-ENDOTOXINS, GENBANK ACCESSION NUMBERS, AND REVISED NOMENCLATURE.sup.A New Old GenBank Accession # ______________________________________ Cry1Aa1 CryIA(a) M11250 Cry1Aa2 CryIA(a) M10917 CryiAa3 CryIA(a) D00348 Cry1Aa4 CryIA(a) X13535 Cry1Aa5 CryIA(a) D17518 Cry1Aa6 CryIA(a) U43605 Cry1Ab1 CryIA(b) M13898 Cry1Ab2 CryIA(b) M12661 Cry1Ab3 CryIA(b) M15271 Cry1Ab4 CryIA(b) D00117 Cry1Ab5 CryIA(b) X04698 Cry1Ab6 CryIA(b) M37263 Cry1Ab7 CryIA(b) X13233 Cry1Ab8 CryIA(b) M16463 Cry1Ab9 CryIA(b) X54939 Cry1Ab10 CryIA(b) Cry1Ac1 CryIA(c) M11068 Cry1Ac2 CryIA(c) M35524 Cry1Ac3 CryIA(c) X54159 Cry1Ac4 CryIA(c) M73249 Cry1Ac5 CryIA(c) M73248 Cry1Ac6 CryIA(c) U43606 Cry1Ac7 CryIA(c) U87793 Cry1Ac8 CryIA(c) U87397 Cry1Ac9 CryIA(c) U89872 Cry1Ac10 CryIA(c) AJ002514 Cry1Ad1 CryIA(d) M73250 Cry1Ae1 CryIA(e) M65252 Cry1Ba1 CryIB X06711 Cry1Ba2 X95704 Cry1Bb1 ET5 L32020 Cry1Bc1 CryIb(c) Z46442 Cry1Bd1 CryE1 Cry1Ca1 CryIC X07518 Cry1Ca2 CryIC X13620 Cry1Ca3 CryIC M73251 Cry1Ca4 CryIC A27642 Cry1Ca5 CryIC X96682 Cry1Ca6 CryIC X96683 Cry1Ca7 CryIC X96684 Cry1Cb1 CryIC(b) M97880 Cry1Da1 CryID X54160 Cry1Db1 PrtB Z22511 Cry1Ea1 CryIE X53985 Cry1Ea2 CryIE X56144 Cry1Ea3 CryIE M73252 Cry1Ea4 U94323 Cry1Eb1 CryIE(b) M73253 Cry1Fa1 CryIF M63897 Cry1Fa2 CryIF M63897 Cry1Fb1 PrtD Z22512 Cry1Ga1 PrtA Z22510 Cry1Ga2 CryIM Y09326 Cry1Gb1 CryH2 Cry1Ha1 PrtC Z22513 Cry1Hb1 U35780 Cry1Ia1 CryV X62821 Cry1Ia2 CryV M98544 Cry1Ia3 CryV L36338 Cry1Ia4 CryV L49391 Cry1Ia5 CryV Y08920 Cry1Ib1 CryV U07642 Cry1Ja1 ET4 L32019 Cry1Jb1 ET1 U31527 Cry1Ka1 U28801 Cry2Aa1 CryIIA M31738 Cry2Aa2 CryIIA M23723 Cry2Aa3 D86084 Cry2Ab1 CryIIB M23724 Cry2Ab2 CryIIB X55416 Cry2Ac1 CryIIC X57252 Cry3Aa1 CryIIIA M22472 Cry3Aa2 CryIIIA J02978 Cry3Aa3 CryIIIA Y00420 Cry3Aa4 CryIIIA M30503 Cry3Aa5 CryIIIA M37207 Cry3Aa6 CryIIIA U10985 Cry3Ba1 CryIIIB X17123 Cry3Ba2 CryIIIB A07234 Cry3Bb1 CryIIIB2 M89794 Cry3Bb2 CryIIIC(b) U31633 Cry3Ca1 CryIIID X59797 Cry4Aa1 CryIVA Y00423 Cry4Aa2 CryIVA D00248 Cry4Ba1 CryIVB X07423 Cry4Ba2 CryIVB X07082 Cry4Ba3 CryIVB M20242 Cry4Ba4 CryIVB D00247 Cry5Aa1 CryVA(a) L07025 Cry5Ab1 CryVA(b) L07026 Cry5Ba1 PS86Q3 U19725 Cry6Aa1 CryVIA L07022 Cry6Ba1 CryVIB L07024 Cry7Aa1 CryIIIC M64478 Cry7Ab1 CryIIICb U04367 Cry8Aa1 CryIIIE U04364 Cry8Ba1 CryIIIG U04365 Cry8Ca1 CryIIIF U04366 Cry9Aa1 CryIG X58120 Cry9Aa2 CryIG X58534 Cry9Ba1 CryIX X75019 Cry9Ca1 CryIH Z37527 Cry9Da1 N141 D85560 Cry10Aa1 CryIVC M12662 Cry11Aa1 CryIVD M31737 Cry11Aa2 CryIVD M22860 Cry11Ba1 Jeg80 X86902 Cry12Aa1 CryVB L07027 Cry13Aa1 CryVC L07023 Cry14Aa1 CryVD U13955 Cry15Aa1 34kDa M76442 Cry16Aa1 cbm71 X94146 Cry17Aa1 cbm71 X99478 Cry18Aa1 CryBP1 X99049 Cry19Aa1 Jeg65 Y08920 Cry20Aa1 U82518 Cry21Aa1 I32932 Cry22Aa1 I34547 Cyt1Aa1 CytA X03182 Cyt1Aa2 CytA X04338 Cyt1Aa3 CytA Y00135 Cyt1Aa4 CytA M35968 Cyt1Ab1 CytM X98793 Cyt1Ba1 U37196 Cyt2Aa1 CytB Z14147 Cyt2Ba1 "CytB" U52043 Cyt2Ba2 "CytB" AF020789 Cyt2Ba3 "CytB" AF022884 Cyt2Ba4 "CytB" AF022885 Cyt2Ba5 "CytB" AF022886 Cyt2Bb1 U82519 ______________________________________ .sup.a Adapted from: http://epunix.biols.susx.ac.uk/Home/Neil.sub.-- Crickmore/Bt/index.html
The utility of bacterial crystal proteins as insecticides was extended beyond lepidopterans and dipteran larvae when the first isolation of a coleopteran-toxic B. thuringiensis strain was reported (Krieg et al., 1983; 1984). This strain (described in U.S. Pat. No. 4,766,203, specifically incorporated herein by reference), designated B. thuringiensis var. tenebrionis, is reported to be toxic to larvae of the coleopteran insects Agelastica alni (blue alder leaf beetle) and Leptinotarsa decemlineata (Colorado potato beetle).
U.S. Pat. No. 5,024,837 also describes hybridB. thuringiensis var. kurstaki strains which showed activity against lepidopteran insects. U.S. Pat. No. 4,797,279 (corresponding to EP 0221024) discloses a hybrid B. thuringiensis containing a plasmid from B. thuringiensis var. kurstaki encoding a lepidopteran-toxic crystal protein-encoding gene and a plasmid from B. thuringiensis tenebrionis encoding a coleopteran-toxic crystal protein-encoding gene. The hybrid B. thuringiensis strain produces crystal proteins characteristic of those made by both B. thuringiensis kurstaki and B. thuringiensis tenebrionis. U.S. Pat. No. 4,910,016 (corresponding to EP 0303379) discloses a B. thuringiensis isolate identified as B. thuringiensis MT 104 which has insecticidal activity against coleopterans and lepidopterans.
The revolution in molecular genetics over the past decade has facilitated a logical and orderly approach to engineering proteins with improved properties. Site specific and random mutagenesis methods, the advent of polymerase chain reaction (PCR™) methodologies, and related advances in the field have permitted an extensive collection of tools for changing both amino acid sequence, and underlying genetic sequences for a variety of proteins of commercial, medical, and agricultural interest.
Following the rapid increase in the number and types of crystal proteins which have been identified in the past decade, researchers began to theorize about using such techniques to improve the insecticidal activity of various crystal proteins. In theory, improvements to δ-endotoxins should be possible using the methods available to protein engineers working in the art, and it was logical to assume that it would be possible to isolate improved variants of the wild-type crystal proteins isolated to date. By strengthening one or more of the aforementioned steps in the mode of action of the toxin, improved molecules should provide enhanced activity, and therefore, represent a breakthrough in the field. If specific amino acid residues on the protein are identified to be responsible for a specific step in the mode of action, then these residues can be targeted for mutagenesis to improve performance.
The combination of structural analyses of B. thuringiensis toxins followed by an investigation of the function of such structures motifs, and the like has taught that specific regions of crystal protein endotoxins are, in a general way, responsible for particular functions.
1.3 Deficiencies in the Prior Art
Unfortunately, while many laboratories have attempted to make mutated crystal proteins, few have succeeded in making mutated crystal proteins with improved lepidopteran toxicity. In almost all of the examples of genetically-engineered B. thuringiensis toxins in the literature, the biological activity of the mutated crystal protein is no better than that of the wild-type protein, and in many cases, the activity is decreased or destroyed altogether (Almond and Dean, 1993; Aronson et al., 1995; Chen et al., 1993, Chen et al., 1995; Ge et al., 1991; Kwak et al., 1995; Lu et al., 1994; Rajamohan et al., 1995; Rajamohan et al., 1996; Smedley and Ellar, 1996; Smith and Ellar, 1994; Wolfersberger et al., 1996; Wu and Aronson, 1992).
For a crystal protein having approximately 650 amino acids in the sequence of its active toxin, and the possibility of 20 different amino acids at each position in this sequence, the likelihood of arbitrarily creating a successful new structure is remote, even if a general function to a stretch of 250-300 amino acids can be assigned. Indeed, the above prior art with respect to crystal protein gene mutagenesis has been concerned primarily with studying the structure and function of the crystal proteins, using mutagenesis to perturb some step in the mode of action, rather than with engineering improved toxins.
Collectively, the limited successes in the art to develop synthetic toxins with improved insecticidal activity have stifled progress in this area and confounded the search for improved endotoxins or crystal proteins. Rather than following simple and predictable rules, the successful engineering of an improved crystal protein may involve different strategies, depending on the crystal protein being improved and the insect pests being targeted. Thus, the process is highly empirical.
Accordingly, traditional recombinant DNA technology is clearly not routine experimentation for providing improved insecticidal crystal proteins. What are lacking in the prior art are rational methods for producing genetically-engineered B. thuringiensis crystal proteins that have improved insecticidal activity and, in particular, improved toxicity towards a wide range of lepidopteran insect pests.
The present invention seeks to overcome these and other drawbacks inherent in the prior art by providing genetically-engineered modified B. thuringiensis δ-endotoxins (Cry*), and in particular modified Cry3 δ-endotoxins (designated Cry3* endotoxins). Also provided are nucleic acid sequences comprising one or more genes which encode such modified proteins. Particularly preferred genes include cry3* genes such as cry3A*, cry3B*, and cry3C* genes, particularly cry3B* genes, and more particularly, cry3Bb* genes, that encode modified crystal proteins having improved insecticidal activity against target pests.
Also disclosed are novel methods for constructing synthetic Cry3* proteins, synthetically-modified nucleic acid sequences encoding such proteins, and compositions arising therefrom. Also provided are synthetic cry3* expression vectors and various methods of using the improved genes and vectors. In a preferred embodiment, the invention discloses and claims Cry3B* proteins and cry3B* genes which encode improved insecticidal polypeptides.
In preferred embodiments, channel-forming toxin design methods are disclosed which have been used to produce a specific set of designed Cry3Bb* toxins with improved biological activity. These improved Cry3Bb* proteins are listed in Table 2 along with their respective amino acid changes from wild-type (WT) Cry3Bb, the nucleotide changes present in the altered cry3Bb* gene encoding the protein, the fold increase in bioactivity over WT Cry3Bb, the structural site of the alteration, and the design method(s) used to create the new toxins.
Accordingly, the present invention provides in an overall and general sense, mutagenized Cry3 protein-encoding genes and methods of making and using such genes. As used herein the term "mutagenized cry3 gene(s)" means one or more cry3 genes that have been mutagenized or altered to contain one or more nucleotide sequences which are not present in the wild type sequences, and which encode mutant Cry3 crystal proteins (Cry3*) showing improved insecticidal activity. Such mutagenized cry3 genes have been referred to in the Specification as cry3* genes. Exemplary cry3* genes include cry3A*, cry3B*, and cry3C* genes.
Exemplary mutagenized Cry3 protein-encoding genes include cry3B genes. As used herein the term "mutagenized cry3B gene(s)" means one or more genes that have been mutagenized or altered to contain one or more nucleotide sequences which are not present in the wild type sequences, and which encode mutant Cry3B crystal proteins (Cry3B*) showing improved insecticidal activity. Such genes have been designated cry3B* genes. Exemplary cry3B* genes include cry3Ba* and cry3Bb* genes, which encode Cry3Ba* and Cry3Bb* proteins, respectively.
Likewise, the present invention provides mutagenized Cry3A protein-encoding genes and methods of making and using such genes. As used herein the term "mutagenized cry3A gene(s)" means one or more genes that have been mutagenized or altered to contain one or more nucleotide sequences which are not present in the wild type sequences, and which encode mutant Cry3A crystal proteins (Cry3A*) showing improved insecticidal activity. Such mutagenized genes have been designated as cry3A* genes.
In similar fashion, the present invention provides mutagenized Cry3C protein-encoding genes and methods of making and using such genes. As used herein the term "mutagenized cry3C gene(s)" means one or more genes that have been mutagenized or altered to contain one or more nucleotide sequences which are not present in the wild type sequences, and which encode mutant Cry3C crystal proteins (Cry3C*) showing improved insecticidal activity. Such mutagenized genes have been designated as cry3C* genes.
Preferably the novel sequences comprise nucleic acid sequences in which at least one, and preferably, more than one, and most preferably, a significant number, of wild-type cry3 nucleotides have been replaced with one or more nucleotides, or where one or more nucleotides have been added to or deleted from the native nucleotide sequence for the purpose of altering, adding, or deleting the corresponding amino acids encoded by the nucleic acid sequence so mutagenized. The desired result, therefore, is alteration of the amino acid sequence of the encoded crystal protein to provide toxins having improved or altered activity and/or specificity compared to that of the unmodified crystal protein.
Examples of preferred Cry2Bb*-encoding genes include cry3Bb.60, cry3Bb.11221, cry3Bb.11222, cry3Bb.11223, cry3Bb.11224, cry3Bb.11225, cry3Bb.11226, cry3Bb.11227, cry3Bb.11228, cry3Bb.11229, cry3Bb.11230, cry3Bb.11231, cry3Bb.11232, cry3Bb.11233, cry3Bb.11234, cry3Bb.11235, cry3Bb.11236, cry3Bb.11237, cry3Bb.11238, cry3Bb.11239, cry3Bb.11241, cry3Bb.11242, cry3Bb.11032, cry3Bb.11035, cry3Bb.11036, cry3Bb.11046, cry3Bb.11048, cry3Bb.11051, cry3Bb.11057, cry3Bb.11058, cry3Bb.11081, cry3Bb.11082, cry3Bb.11083, cry3Bb.11084, cry3Bb.11095, and cry3Bb.11098.
TABLE 2
__________________________________________________________________________
CRY3BB* PROTEINS EXHIBITING IMPROVED ACTIVITY AGAINST SCRW LARVAE
Cry3Bb*
cry3Bb* Fold Design
Protein
Plasmid
cry3Bb* Nucleotide Sequence
Cry3Bb* Amino
Structural Site
Increase Over
Method
Designation
Designation
Changes Acid Changes
of Changes
WT Activity
Used
__________________________________________________________________________
Cry3Bb.60
-- -- Δ1-159
Δα1-α3
3.6×
1, 6, 8
Cry3Bb.11221
pEG1707
A460T, C461T, A462T, C464A,
T154F, P155H,
1α3,4
6.4×
1, 8
T465C, T466C, T467A, A468T,
L156H, L158R
A469T, G470C, T472C, T473G,
G474T, A477T, A478T, G479C
Cry3Bb.11222
pEG1708
T687C, T688C, A689T, C691A,
Y230L, H231S
α6
4.0×
3, 7
A692G
Cry3Bb.11223
pEG1709
T667C, T687C, T688A, A689G,
S223P, Y230S
α6
2.8×
3
C691A, A692G
Cry3Bb.11224
pEG1710
T687C, A692G H231R α6
5.0×
Cry3Bb.11225
pEG1711
T687C, C691A H231N, T241S
α6
3.6×
Cry3Bb.11226
pEG1712
T687C, C691A, A692C, T693C
H231T α6
3.0×
7, 8
Cry3Bb.11227
pEG1713
C868A, G869A, G870T
R290N 1α7,β1
1.9×
2, 3, 4 6
Cry3Bb.11228
pEG1714
C932T, A938C, T942G, G949A,
S311L, N313T,
1β1,α8
4.1×
2, 4
T954C E317K
Cry3Bb.11229
pEG1715
T931A, A933C, T942A, T945A,
S311T, E317K,
1β1,α8
2.5×
2, 4
G949A, A953G, T954C
Y318C
Cry3Bb.11230
pEG1716
T931G, A933C, C934G, T945G,
S311A, L312V,
1β1,α8
4.7×
2, 4 8
C946T, A947G, G951A, T954C
Q316W
Cry3Bb.11231
pEG1717
T687C, A692G, C932T, A938C,
H231R, S311L,
α6; 1β1,α8
7.9×
2, 4, 7, 8,
T942G, G949A, T954C
N313T, E317K 10
Cry3Bb.11232
pEG1718
T931A, A933G, T935C, T936A,
S311T, L312P,
1β1,α8
5.1×
4
A938C, T939C, T942C, T945A,
N313T, E317N
G951T, T954C
Cry3Bb.11233
pEG1719
T931G, A933C, T936G, T942C,
S311A, Q316D
1β1,α8
2.2×
2, 4
C943T, T945A, C946G, G948C,
T954C
Cry3Bb.11234
pEG1720
T861C, T866C, C868A, T871C,
I289T, L291R,
1α7,β1
4.1×
4
T872G, A875T, T877A, C878G,
Y292F, S293R
A882G
Cry3Bb.11235
pEG1721
T687C, A692G, C932T
H231R, S311L
α6; 1β1,α8
3.2×
2, 4, 7, 8,
10
Cry3Bb.11236
pEG1722
T931A, C932T, A933C, T936C,
S311I 1β1,α8
3.1×
2, 4
T942G, T945A, T954C
Cry3Bb.11237
pEG1723
T931A, C932T, A933C, T936C,
S311I, N313H
1β1,α8
5.4×
2, 4
A937G, A938T, C941A, T942C,
T945A, C946A, A947T, A950T,
T954C
Cry3Bb.11238
pBG1724
A933C, T936C, A937G, A938T,
N313V, T314N,
1β1,α8
2.6×
2, 4
C941A, T942C, T945A, C946A,
Q316M, E317V
A947T, A950T, T954C
Cry3Bb.11239
pEG1725
A933T, A938G, T939G, T942A,
N313R, L315P,
1β1,α8
2.8×
2, 4
T944C, T945A, A947T, G948T,
Q316L, E317A
A950C, T954C
Cry3Bb.11241
pBG1726
A860T, T861C, G862A, C868T,
Y287F, D288N,
1α7,β1
2.6×
2, 3, 4, 6
G869T, T871C, A873T, T877A,
R290L
C878G, A879T
Cry3Bb.11242
pEG1727
C868G, G869T R290V 1α7,β1
2.5×
2, 3, 4, 6,
8
Cry3Bb.11032
pEG1041
A494G D165G α4
3.1×
2, 4, 8
Cry3Bb.11035
pEG1046
G479A, A481C, A482C,
S160N, K161P,
α4
2.7×
8
A484C, G485A, A486C, A494G
P162H, D165G
Cry3Bb.11036
pEG1047
A865G, T877C 1289V, S293P
1α7,β1
4.3×
4
Cry3Bb.11046
pEG1052
G479A, A481C, A482C,
S160N, K161P,
α4; 1α7,β1
2.6×
2, 4, 8, 10
A484C, G485A, A486C,
P162H, D165G,
A494G, A865G, T877C
I289V, S293P
Cry3Bb.11048
pEG1054
T309A, Δ310, Δ311, Δ312
D103E, ΔA104
1α2a,2b
4.3×
8
Cry3Bb.11051
pEG1057
A565G, A566G K189G 1α4,5
3.0×
2, 3, 4
Cry3Bb.11057
pEG1062
T309A, Δ310, Δ311, Δ312,
D103E, ΔA104,
1α2a,2b; α4
3.4×
2, 4, 8, 10
G479A, A481C, A482C,
S160N, K161P,
A484C, G485A, A486C, A494G
P162H, D165G
Cry3Bb.11058
pEG1063
T309A, Δ310, Δ311, Δ312,
D103E, ΔA104,
1α2a,2b; 1α3,4
3.5×
1, 8, 10
A460T, C461T, A462T, C464A,
T154F, P155H,
T465C, T466C, T467A, A468T,
L156H, L158R
A469T, G470C, T472C, T473G,
G474T, A477T, A478T, G479C
Cry3Bb.11081
pEG1084
A494G, T931A, A933C, T942A,
D165G, S311T,
α4; 1β1,α8
6.1×
2, 4, 8, 10
T945A, G949A, T954C
E317K
Cry3Bb.11082
pEG1085
A494G, A865G, T877C, T914C,
D165G, I289V,
α4; 1α7,β1;
4.9×
2, 4, 5, 8
T931G, A933C, C934G, T945G,
S293P, F305S,
1β1,α8; β2;
9, 10
C946T, A947G, G951A, T954C,
S311A, L312V,
β3b
A1043G, T1094C Q316W, Q348R,
V365A
Cry3Bb.11083
pEG1086
A865G, T877C, A1043G
1289V, S293P,
1α7,β1; β2
7.4×
4, 5, 9, 10
Q348R
Cry3Bb.11084
pEG1087
A494G, C932T D165G, S311L
α4; 1β1,
7.2×
2, 4, 8, 10
Cry3Bb.11095
pEG1095
A1043G Q348R β2 4.6×
5, 9
Cry3Bb.11098
pEG1098
A494G, T687C, A692G, C932T,
D165G, H231R,
α4; α6, 1β1,
α8
7.9×
2, 4, 7, 8
A938C, T942G, G949A, T954C
S311L, N313T,
E317K
__________________________________________________________________________
In a variety of illustrative embodiments, the inventors have shown remarkable success in generating toxins with improved insecticidal activity using these methods. In particular, the inventors have identified unique methods of analyzing and designing toxins having improved or enhanced insecticidal properties both in vitro and in vivo.
In addition to modifications of Cry3Bb peptides, those having benefit of the present teaching are now also able to make mutations in a variety of channel-forming toxins, and particularly in crystal proteins which are related to Cry3Bb either functionally or structurally. In fact, the inventors contemplate that any B. thuringiensis crystal protein or peptide can be analyzed using the methods disclosed herein and may be altered using the methods disclosed herein to produce crystal proteins having improved insecticidal specificity or activity. Alternatively, the inventors contemplate that those of skill in the art having the benefit of the teachings disclosed herein will be able to prepare not only mutated Cry3 toxins with improved activity, but also other crystal proteins including all of those proteins identified in Table 1, herein. In particular, the inventors contemplate the creation of Cry3* variants using one or more of the methods disclosed herein to produce toxins with improved activity. For example, the inventors note Cry3A, Cry3B, and Cry3C crystal proteins (which are known in the art) may be modified using one or more of the design strategies employed herein, to prepare synthetically-modified crystal proteins with improved properties. Likewise, one of skill in the art will even be able to utilize the teachings of the present disclosure to modify other channel forming toxins, including channel forming toxins other than B. thuringiensis crystal proteins, and even to modify proteins and channel toxins not yet described or characterized.
Because the structures for insecticidal crystal proteins show a remarkable conservation of protein tertiary structure (Grochulski et al., 1995), and because many crystal proteins show significant amino acid sequence identity to the Cry3Bb amino acid sequence within domain 1, including proteins of the cry1, Cry2, Cry3, Cry4, Cry5, Cry7, Cry8, Cry9, cry10, cry11, cry12, cry13, cry14, and cry16 classes (Table 1), now in light of the inventors' surprising discovery, for the first time, those of skill in the art having benefit of the teachings disclosed herein will be able to broadly apply the methods of the invention to modifying a host of crystal proteins with improved activity or altered specificity. Such methods will not only be limited to the insecticidal crystal proteins disclosed in Table 1, but may also been applied to any other related crystal protein, including those yet to be identified.
In particular, the high degree of homology between Cry3A, Cry3B, and Cry3C proteins is evident in the alignment of the primary amino acid sequence of the three proteins (FIG. 17A, FIG. 17B, and FIG. 17C).
As such, the disclosed methods may be now applied to preparation of modified crystal proteins having one or more alterations introduced using one or more of the mutational design methods as disclosed herein. The inventors further contemplate that regions may be identified in one or more domains of a crystal protein, or other channel forming toxin which may be similarly modified through site-specific or random mutagenesis to generate toxins having improved activity, or alternatively, altered specificity.
In certain applications, the creation of altered toxins having increased activity against one or more insects is desired. Alternatively, it may be desirable to utilize the methods described herein for creating and identifying altered insecticidal crystal proteins which are active against a wider spectrum of susceptible insects. The inventors further contemplate that the creation of chimeric insecticidal crystal proteins comprising one or more of these mutations may be desirable for preparing "super" toxins which have the combined advantages of increased insecticidal activity and concomitant broad spectrum activity.
In light of the present disclosure, the mutagenesis of one or more codons within the sequence of a toxin may result in the generation of a host of related insecticidal proteins having improved activity. While exemplary mutations have been described for each of the design strategies employed in the present invention, the inventors contemplate that mutations may also be made in insecticidal crystal proteins, including the loop regions, helices regions, active sites of the toxins, regions involved in protein oligomerization, and the like, which will give rise to functional bioinsecticidal crystal proteins. All such mutations are considered to fall within the scope of this disclosure.
In one illustrative embodiment, mutagenized cry3Bb* genes are obtained which encode Cry3Bb* variants that are generally based upon the wild-type Cry3Bb sequence, but that have one or more changes incorporated into the amino acid sequence of the protein using one or more of the design strategies described and claimed herein.
In these and other embodiments, the mutated genes encoding the crystal proteins may be modified so as to change about one, two, three, four, or five or so amino acids in the primary sequence of the encoded polypeptide. Alternatively even more changes from the native sequence may be introduced, such that the encoded protein may have at least about 1% or 2%, or alternatively about 3% or about 4%, or even about 5% to about 10%, or about 10% to about 15%, or even about 15% to about 20% or more of the codons either altered, deleted, or otherwise modified. In certain situations, it may even be desirable to alter substantially more of the primary amino acid sequence to obtain the desired modified protein. In such cases the inventors contemplate that from about 25%, to about 50%, or even from about 50% to about 75%, or more of the native (or wild-type) codons either altered, deleted, or otherwise modified. Alternatively, mutations in the amino acid sequences or underlying DNA gene sequences which result in the insertion or deletion of one or more amino acids within one or more regions of the crystal protein or peptide.
To effect such changes in the primary sequence of the encoded polypeptides, it may be desirable to mutate or delete one or more nucleotides from the nucleic acid sequences of the genes encoding such polypeptides, or alternatively, under certain circumstances to add one or more nucleotides into the primary nucleic acid sequence at one or more sites in the sequence. Frequently, several nucleotide residues may be altered to produce the desired polypeptide. As such, the inventors contemplate that in certain embodiments it may be desirable to alter only one, two, three, four, or five or so nucleotides in the primary sequence. In other embodiments, which more changes are desired, the mutagenesis may involve changing, deleting, or inserting 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, or even 20 or so nucleotide residues in the gene sequence. In still other embodiments, one may desire to mutate, delete, or insert 21, 22, 23, 24, 25, 26, 27, 28, 29, 30-40, 40-50, 50-60, 60-70, 70-80, 80-90, or even 90-100, 150, 200, 250, 300, 350, 400, 450, or more nucleotides in the sequence of the gene in order to prepare a cry3* gene which produces a Cry3* polypeptide having the desired characteristics. In fact, any number of mutations, deletions, and/or insertions may be made in the primary sequence of the gene, so long as the encoded protein has the improved insecticidal activity or specificity characteristics described herein.
Changing a large number of the codons in the nucleotide sequence of an endotoxin-encoding gene may be particularly desirable and often necessary to achieve the desired results, particularly in the situation of "plantizing" a DNA sequence in order to express a DNA of non-plant origin in a transformed plant cell. Such methods are routine to those of skill in the plant genetics arts, and frequently many residues of a primary gene sequence will be altered to facilitate expression of the gene in the plant cell. Preferably, the changes in the gene sequence introduce no changes in the amino acid sequence, or introduce only conservative replacements in the amino acid sequence such that the polypeptide produced in the plant cell from the "plantized" nucleotide sequence is still fully functional, and has the desired qualities when expressed in the plant cell.
Genes and encoded proteins mutated in the manner of the invention may also be operatively linked to other protein-encoding nucleic acid sequences, or expressed as fusion proteins. Both N-terminal and C-terminal fusion proteins are contemplated. Virtually any protein- or peptide-encoding DNA sequence, or combinations thereof, may be fused to a mutated cry3* sequence in order to encode a fusion protein. This includes DNA sequences that encode targeting peptides, proteins for recombinant expression, proteins to which one or more targeting peptides is attached, protein subunits, domains from one or more crystal proteins, and the like. Such modifications to primary nucleotide sequences to enhance, target, or optimize expression of the gene sequence in a particular host cell, tissue, or cellular localization, are well-known to those of skill in the art of protein engineering and molecular biology, and it will be readily apparent to such artisans, having benefit of the teachings of this specification, how to facilitate such changes in the nucleotide sequence to produce the polypeptides and polynucleotides disclosed herein.
In one aspect, the invention discloses and claims host cells comprising one or more of the modified crystal proteins disclosed herein, and in particular, cells of B. thuringiensis strains EG11221, EG11222, EG11223, EG11224, EG11225, EG11226, EG11227, EG11228, EG11229, EG11230, EG11231, EG11232, EG11233, EG11234, EG11235, EG11236, EG11237, EG11238, EG11239, EG11241, EG11242, EGI111032, EG11035, EG11036, EG11046, EG11048, EG11051, EG11057, EG11058, EG11081, EG11082, EG11083, EG11084, EG11095, and EG11098 which comprise recombinant DNA segments encoding synthetically-modified Cry3Bb* crystal proteins which demonstrates improved insecticidal activity.
Likewise, the invention also discloses and claims cell cultures of B. thuringiensis EG11221, EG11222, EG11223, EG11224, EG11225, EG11226, EG11227, EG11228, EG11229, EG11230, EG11231, EG11232, EG11233, EG11234, EG11235, EG11236, EG11237, EG11238, EG11239, EG11241, EG11242, EG11032, EG11035, EG11036, EG11046, EG11048, FG11051, EG11057, EG11058, EG11081, EG11082, EG11083, EG11084, and EG11095, and 11098.
Such cell cultures may be biologically-pure cultures consisting of a single strain, or alternatively may be cell co-cultures consisting of one or more strains. Such cell cultures may be cultivated under conditions in which one or more additional B. thuringiensis or other bacterial strains are simultaneously co-cultured with one or more of the disclosed cultures, or alternatively, one or more of the cell cultures of the present invention may be combined with one or more additional B. thuringiensis or other bacterial strains following the independent culture of each. Such procedures may be useful when suspensions of cells containing two or more different crystal proteins are desired.
The subject cultures have been deposited under conditions that assure that access to the cultures will be available during the pendency of this patent application to one determined by the Commissioner of Patents and Trademarks to be entitled thereto under 37 C.F.R. §1.14 and 35 U.S.C. §122. The deposits are available as required by foreign patent laws in countries wherein counterparts of the subject application, or its progeny, are filed. However, it should be understood that the availability of a deposit does not constitute a license to practice the subject invention in derogation of patent rights granted by governmental action.
Further, the subject culture deposits will be stored and made available to the public in accord with the provisions of the Budapest Treaty for the Deposit of Microorganisms, i.e., they will be stored with all the care necessary to keep them viable and uncontaminated for a period of at least five years after the most recent request for the finishing of a sample of the deposit, and in any case, for a period of at least 30 (thirty) years after the date of deposit or for the enforceable life of any patent which may issue disclosing the cultures. The depositor acknowledges the duty to replace the deposits should the depository be unable to furnish a sample when requested, due to the condition of the deposits. Al restrictions on the availability to the public of the subject culture deposits will be irrevocably removed upon the granting of a patent disclosing them.
Cultures shown in Table 3 were deposited in the permanent collection of the Agricultural Research Service Culture Collection, Northern Regional Research Laboratory (NRRL) under the terms of the Budapest Treaty.
TABLE 3
______________________________________
STRAINS OF THE PRESENT INVENTION DEPOSITED UNDER
THE TERMS OF THE BUDAPEST TREATY
Accession Number
Strain Deposit Date
Protein (NRRL Number)
______________________________________
EG11032 5/27/97 Cry3Bb.11032
B-21744
EG11035 5/27/97 Cry3Bb.11035
B-21745
EG11036 5/27/97 Cry3Bb.11036
B-21746
EG11037 5/27/97 Cry3Bb.11037
B-21747
EG11046 5/27/97 Cry3Bb.11046
B-21748
EG11048 5/27/97 Cry3Bb.11048
B-21749
EG11051 5/27/97 Cry3Bb.11051
B-21750
EG11057 5/27/97 Cry3Bb.11057
B-21751
EG11058 5/27/97 Cry3Bb.11058
B-21752
EG11081 5/27/97 Cry3Bb.11081
B-21753
EG11082 5/27/97 Cry3Bb.11082
B-21754
EG11083 5/27/97 Cry3Bb.11083
B-21755
EG11084 5/27/97 Cry3Bb.11084
B-21756
EG11095 5/27/97 Cry3Bb.11095
B-21757
EG11204 5/27/97 Cry3Bb.11204
B-21758
EG11221 5/27/97 Cry3Bb.11221
B-21759
EG11222 5/27/97 Cry3Bb.11222
B-21760
EG11223 5/27/97 Cry3Bb.11223
B-21761
EG11224 5/27/97 Cry3Bb.11224
B-21762
EG11225 5/27/97 Cry3Bb.11225
B-21763
EG11226 5/27/97 Cry3Bb.11226
B-21764
EG11227 5/27/97 Cry3Bb.11227
B-12765
EG11228 5/27/97 Cry3Bb.11228
B-12766
EG11229 5/27/97 Cry3Bb.11229
B-21767
EG11230 5/27/97 Cry3Bb.11230
B-21768
EG11231 5/27/97 Cry3Bb.11231
B-21769
EG11232 5/27/97 Cry3Bb.11232
B-12770
EG11233 5/27/97 Cry3Bb.11233
B-21771
EG11234 5/27/97 Cry3Bb.11234
B-21772
EG11235 5/27/97 Cry3Bb.11235
B-21773
EG11236 5/27/97 Cry3Bb.11236
B-21774
EG11237 5/27/97 Cry3Bb.11237
B-21775
EG11238 5/27/97 Cry3Bb.11238
B-21776
EG11239 5/27/97 Cry3Bb.11239
B-21777
EG11241 5/27/97 Cry3Bb.11241
B-21778
EG11242 5/27/97 Cry3Bb.11242
B-21779
______________________________________
Also disclosed are methods of controlling or eradicating an insect population from an environment. Such methods generally comprise contacting the insect population to be controlled or eradicated with an insecticidally-effective amount of a Cry3* crystal protein composition. Preferred Cry3* compositions include Cry3A*, Cry3B*, and Cry3C* polypeptide compositions, with Cry3B* compositions being particularly preferred. Examples of such polypeptides include proteins selected from the group consisting of Cry3Bb-60, Cry3Bb.11221, Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11234, Cry3Bb.11235, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11032, Cry3Bb.11035, Cry3Bb.11036, Cry3Bb.11046, Cry3Bb.11048, Cry3Bb.11051, Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11095, and Cry3Bb.11098.
In preferred embodiments, these Cry3Bb* crystal protein compositions comprise the amino acid sequence of any of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6. SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14. SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102 or SEQ ID NO:108.
The modified Cry* polypeptides of the present invention are preparable by a process which generally involves the steps of obtaining a nucleic acid sequence encoding a Cry* polypeptide; analyzing the structure of the polypeptide to identify particular "target" sites for mutagenesis of the underlying gene sequence; introducing one or more mutations into the nucleic acid sequence to produce a change in one or more amino acid residues in the encoded polypeptide sequence; and expressing in a transformed host cell the mutagenized nucleic acid sequence under conditions effective to obtain the modified Cry* protein encoded by the cry* gene.
Means for obtaining the crystal structures of the polypeptides of the invention are well-known. Exemplary high resolution crystal structure solution sets are given in Section 9.0 of the disclosure, and include the crystal structure of both the Cry3A and Cry3B polypeptides disclosed herein. The information provided in Section 9.0 permits the analyses disclosed in each of the methods herein which rely on the 3D crystal structure information for targeting mutagenesis of the polypeptides to particular regions of the primary amino acid sequences of the δ-endotoxins to obtain mutants with increased insecticidal activity or enhanced insecticidal specificity.
A first method for producing a modified B. thuringiensis Cry3Bb δ-endotoxin having improved insecticidal activity or specificity disclosed herein generally involves obtaining a high-resolution 3D crystal structure of the endotoxin, locating in the crystal structure one or more regions of bound water wherein the bound water forms a contiguous hydrated surfaces separated by no more than about 16 Å; increasing the number of water molecules in this surface by increasing the hydrophobicity of one or more amino acids of the protein in the region; and obtaining the modified δ-endotoxin so produced. Exemplary δ-endotoxins include Cry3Bb.11032, Cry3Bb.11227, Cry3Bb.11241, Cry3Bb.11051, Cry3Bb.11242, and Cry3Bb.11098.
A second method for producing a modified B. thuringiensis Cry3Bb δ-endotoxin having improved insecticidal activity comprises identifying a loop region in a δ-endotoxin; modifying one or more amino acids in the loop to increase the hydrophobicity of the amino acids; and obtaining the modified δ-endotoxin so produced. Preferred δ-endotoxin produced by this method include Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11233, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, and Cry3Bb.11239.
A method for increasing the mobility of channel forming helices of a B. thuringiensis Cry3B δ-endotoxin is also provided by the present invention. The method generally comprises disrupting one or more hydrogen bonds formed between a first amino acid of one or more of the channel forming helices and a second amino acid of the δ-endotoxin. The hydrogen bonds may be formed inter- or intramolecularly, and the disrupting may consist of replacing a first or second amino acid with a third amino acid whose spatial distance is greater than about 3 Å, or whose spatial orientation bond angle is not equal to 180±60 degrees relative to the hydrogen bonding site of the first or second amino acid. δ-endotoxins produced by this method and disclosed herein include Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11231, Cry3Bb.11241, and Cry3Bb.11242, and Cry3Bb.11098.
Also disclosed is a method of increasing the flexibility of a loop region in a channel forming domain of a B. thuringiensis Cry3Bb δ-endotoxin. This method comprises obtaining a crystal structure of a Cry3Bb δ-endotoxin having one or more loop regions; identifying the amino acids comprising the loop region; and altering one or more of the amino acids to reduce steric hindrance in the loop region, wherein the altering increases flexibility of the loop region in the δ-endotoxin. Examples of δ-endotoxins produced using this method include Cry3Bb.11032, Cry3Bb.11051, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11227, Cry3Bb.11234, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11036, and Cry3Bb.11098.
Another aspect of the invention is a method for increasing the activity of a δ-endotoxin, comprising reducing or eliminating binding of the δ-endotoxin to a carbohydrate in a target insect gut. The eliminating or reducing may be accomplished by removal of one or more α helices of domain 1 of the δ-endotoxin, for example, by removal of α helices α1, α2a/b, and α3. An exemplary δ-endotoxin produced using the method is Cry3Bb.60.
Alternatively, the reducing or eliminating may be accomplished by replacing one or more amino acids within loop β1,α8, with one or more amino acids having increased hydrophobicity. Such a method gives rise to δ-endotoxins such as Cry3Bb.11228, Cry3Bb.11230, Cry3B.11231, Cry3Bb.11237, and Cry3Bb.11098, which are described in detail, herein.
Alternatively, the reducing or eliminating is accomplished by replacing one or more specific amino acids, with any other amino acid. Such replacements are described in Table 2, and in the examples herein. One example is the δ-endotoxin designated herein as Cry3Bb.11221.
A method of identifying a region of a Cry3Bb δ-endotoxin for targeted mutagenesis comprising: obtaining a crystal structure of the δ-endotoxin; identifying from the crystal structure one or more surface-exposed amino acids in the protein; randomly substituting one or more of the surface-exposed amino acids to obtain a plurality of mutated polypeptides, wherein at least 50% of the mutated polypeptides have diminished insecticidal activity; and identifying from the plurality of mutated polypeptides one or more regions of the Cry3Bb δ-endotoxin for targeted mutagenesis. The method may further comprise determining the amino acid sequences of a plurality of mutated polypeptides having diminished activity, and identifying one or more amino acid residues required for insecticidal activity.
In another embodiment, the invention provides a process for producing a Cry3Bb δ-endotoxin having improved insecticidal activity. The process generally involves the steps of obtaining a high-resolution crystal structure of the protein; determining the electrostatic surface distribution of the protein; identifying one or more regions of high electrostatic diversity; modifying the electrostatic diversity of the region by altering one or more amino acids in the region; and obtaining a Cry3Bb δ-endotoxin which has improved insecticidal activity. In one embodiment, the electrostatic diversity may be decreased relative to the electrostatic diversity of a native Cry3Bb δ-endotoxin. Exemplary δ-endotoxins with decreased electrostatic diversity include Cry3Bb.11227, Cry3Bb.11241, and Cry3Bb.11242. Alternatively, the electrostatic diversity may be increased relative to the electrostatic diversity of a native Cry3Bb δ-endotoxin. An exemplary δ-endotoxin with increased electrostatic diversity is Cry3Bb.11234.
Furthermore, the invention also provides a method of producing a Cry3Bb δ-endotoxin having improved insecticidal activity which involves obtaining a high-resolution crystal structure; identifying the presence of one or more metal binding sites in the protein; altering one or more amino acids in the binding site; and obtaining an altered protein, wherein the protein has improved insecticidal activity. The altering may involve the elimination of one or more metal binding sites. Exemplary δ-endotoxin include Cry3Bb.11222, Cry3Bb.11224, Cry3Bb.11225, and Cry3Bb.11226.
A further aspect of the invention involves a method of identifying a B. thuringiensis Cry3Bb δ-endotoxin having improved channel activity. This method in an overall sense involves obtaining a Cry3Bb δ-endotoxin suspected of having improved channel activity; and determining one or more of the following characteristics in the δ-endotoxin, and comparing such characteristics to those obtained for the wild-type unmodified δ-endotoxin: (1) the rate of channel formation, (2) the rate of growth of channel conductance or (3) the duration of open channel state. From this comparison, one may then select a δ-endotoxin which has an increased rate of channel formation compared to the wildtype δ-endotoxin. Examples of Cry3Bb δ-endotoxins prepared by this method include Cry3Bb.60, Cry3Bb.11035, Cry3Bb.11048, Cry3Bb.11032, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11226, Cry3Bb.11221, Cry3Bb.11242, Cry3Bb.11230, and Cry3Bb.11098.
Also provided is a method for producing a modified Cry3Bb δ-endotoxin, having improved insecticidal activity which involves altering one or more non-surface amino acids located at or near the point of greatest convergence of two or more loop regions of the Cry3Bb δ-endotoxin, such that the altering decreases the mobility of one or more of the loop regions. The mobility may conveniently be determined by comparing the thermal denaturation of the modified protein to a wild-type Cry3Bb δ-endotoxin. An exemplary crystal protein produced by this method is Cry3Bb.11095.
A further aspect of the invention involves a method for preparing a modified Cry3Bb δ-endotoxin, having improved insecticidal activity comprising modifying one or more amino acids in the loop to increase the hydrophobicity of said amino acids; and altering one or more of said amino acids to reduce steric hindrance in the loop region, wherein the altering increases flexibility of the loop region in the endotoxin. Exemplary Cry3Bb δ-endotoxins produced is selected from the group consisting of Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11231, Cry3Bb.11235, and Cry3Bb.11098.
The invention also provides a method of improving the insecticidal activity of a B. thuringiensis Cry3Bb δ-endotoxin, which generally comprises inserting one or more protease sensitive sites into one or more loop regions of domain 1 of the δ-endotoxin. Preferably, the loop region is α3,4, and an exemplary δ-endotoxin so produced is Cry3Bb.11221.
The crystal proteins so produced by each of the methods described herein also represent important aspects of the invention. Such crystal proteins preferably include a protein or peptide selected from the group consisting of Cry3Bb-60, Cry3Bb.11221, Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11234, Cry3Bb.11235, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11032, Cry3Bb.11035, Cry3Bb.11036, Cry3Bb.11046, Cry3Bb.11048, Cry3Bb.11051, Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11095, and Cry3Bb.11098.
In preferred embodiments, the protein comprises a contiguous amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6. SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14. SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, and SEQ ID NO:108.
Highly preferred are those crystal proteins which are encoded by the nucleic acid sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101; or SEQ ID NO:107, or a nucleic acid sequence which hybridizes to the nucleic acid sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107 under conditions of moderate stringency.
Amino acid, peptide and protein sequences within the scope of the present invention include, and are not limited to the sequences set forth in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22 SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46 SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, and SEQ ID NO:108, and rations in the amino acid sequences including alterations, deletions, mutations, and homologs.
Compositions which comprise from about 0.5% to about 99% by weight of the crystal protein, or more preferably from about 5% to about 75%, or from about 25% to about 50% by weight of the crystal protein are provided herein. Such compositions may readily be prepared using techniques of protein production and purification well-known to those of skill, and the methods disclosed herein. Such a process for preparing a Cry3Bb* crystal protein generally involves the steps of culturing a host cell which expresses the Cry3Bb* protein (such as a B. thuringiensis EG11221, EG11222, EG11223, EG11224, EG11225, EG11226, EG11227, EG11228, EG11229, EG11230, EG11231, EG11232, EG11233, EG11234, EG11235, EG11236, EG11237, EG11238, EG11239, EG11241, EG11242, EG11032, EG11035, EG11036, EG11046, EG11048, EG11051, EG11057, EG11058, EG11081, EG11082, EG11083, EG11084, EG11095, or EG11098 cell) under conditions effective to produce the crystal protein, and then obtaining the crystal protein so produced.
The protein may be present within intact cells, and as such, no subsequent protein isolation or purification steps may be required. Alternatively, the cells may be broken, sonicated, lysed, disrupted, or plasmolyzed to free the crystal protein(s) from the remaining cell debris. In such cases, one may desire to isolate, concentrate, or further purify the resulting crystals containing the proteins prior to use, such as, for example, in the formulation of insecticidal compositions. The composition may ultimately be purified to consist almost entirely of the pure protein, or alternatively, be purified or isolated to a degree such that the composition comprises the crystal protein(s) in an amount of from between about 0.5% and about 99% by weight, or in an amount of from between about 5% and about 95% by weight, or in an amount of from between about 15% and about 85% by weight, or in an amount of from between about 25% and about 75% by weight, or in an amount of from between about 40% and about 60% by weight etc.
One important embodiment of the invention is a recombinant vector which comprises a nucleic acid segment encoding one or more of the novel B. thuringiensis crystal proteins disclosed herein. Such a vector may be transferred to and replicated in a prokaryotic or eukaryotic host, with bacterial cells being particularly preferred as prokaryotic hosts, and plant cells being particularly preferred as eukaryotic hosts.
In preferred embodiments, the recombinant vector comprises a nucleic acid segment encoding the amino acid sequence of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108. Highly preferred nucleic acid segments are those which have the sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107.
Another important embodiment of the invention is a transformed host cell which expresses one or more of these recombinant vectors. The host cell may be either prokaryotic or eukaryotic, and particularly preferred host cells are those which express the nucleic acid segment(s) comprising the recombinant vector which encode one or more B. thuringiensis crystal protein comprising modified amino acid sequences in one or more loop regions of domain 1, or between α helix 7 of domain 1 and β strand 1 of domain 2. Bacterial cells are particularly preferred as prokaryotic hosts, and plant cells are particularly preferred as eukaryotic hosts.
In an important embodiment, the invention discloses and claims a host cell wherein the modified amino acid sequences comprise one or more loop regions between α helices 1 and 2, α helices 2 and 3, α helices 3 and 4, α helices 4 and 5, α helices 5 and 6 or α helices 6 and 7 of domain 1, or between α helix 7 of domain 1 and β strand 1 of domain 2. A particularly preferred host cell is one that comprises the amino acid sequence of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108, and more preferably, one that comprises the nucleic acid sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107.
Bacterial host cells transformed with a nucleic acid segment encoding a modified Cry3Bb crystal protein according to the present invention are disclosed and claimed herein, and in particular, a B. thuringiensis cell having designation EG11221, EG11222, EG11223, EG11224, EG11225, EG11226, EG11227, EG11228, EG11229, EG11230, EG11231, EG11232, EG11233, EG11234, EG11235, EG11236, EG11237, EG11238, EG11239, EG11241, EG11242, EG11032, EG11035, EG11036, EG11046, EG11048, EG11051, EG11057, EG11058, EG11081, EG11082, EG11083, EG11084, EG11095, or EG11098.
In another embodiment, the invention encompasses a method of using a nucleic acid segment of the present invention that encodes a cry3Bb* gene. The method generally comprises the steps of: (a) preparing a recombinant vector in which the cry3Bb* gene is positioned under the control of a promoter; (b) introducing the recombinant vector into a host cell; (c) culturing the host cell under conditions effective to allow expression of the Cry3Bb* crystal protein encoded by said cry3Bb* gene; and (d) obtaining the expressed Cry3Bb* crystal protein or peptide.
A wide variety of ways are available for introducing a B. thuringiensis gene expressing a toxin into the microorganism host under conditions which allow for stable maintenance and expression of the gene. One can provide for DNA constructs which include the transcriptional and translational regulatory signals for expression of the toxin gene, the toxin gene under their regulatory control and a DNA sequence homologous with a sequence in the host organism, whereby integration will occur, and/or a replication system which is functional in the host, whereby integration or stable maintenance will occur.
The transcriptional initiation signals will include a promoter and a transcriptional initiation start site. In some instances, it may be desirable to provide for regulative expression of the toxin, where expression of the toxin will only occur after release into the environment. This can be achieved with operators or a region binding to an activator or enhancers, which are capable of induction upon a change in the physical or chemical environment of the microorganisms. For example, a temperature sensitive regulatory region may be employed, where the organisms may be grown up in the laboratory without expression of a toxin, but upon release into the environment, expression would begin. Other techniques may employ a specific nutrient medium in the laboratory, which inhibits the expression of the toxin, where the nutrient medium in the environment would allow for expression of the toxin. For translational initiation, a ribosomal binding site and an initiation codon will be present.
Various manipulations may be employed for enhancing the expression of the messenger RNA, particularly by using an active promoter, as well as by employing sequences, which enhance the stability of the messenger RNA. The transcriptional and translational termination region will involve stop codon(s), a terminator region, and optionally, a polyadenylation signal. A hydrophobic "leader" sequence may be employed at the amino terminus of the translated polypeptide sequence in order to promote secretion of the protein across the inner membrane.
In the direction of transcription, namely in the 5' to 3' direction of the coding or sense sequence, the construct will involve the transcriptional regulatory region, if any, and the promoter, where the regulatory region may be either 5' or 3' of the promoter, the ribosomal binding site, the initiation codon, the structural gene having an open reading frame in phase with the initiation codon, the stop codon(s), the polyadenylation signal sequence, if any, and the terminator region. This sequence as a double strand may be used by itself for transformation of a microorganism host, but will usually be included with a DNA sequence involving a marker, where the second DNA sequence may be joined to the toxin expression construct during introduction of the DNA into the host.
By a marker is intended a structural gene which provides for selection of those hosts which have been modified or transformed. The marker will normally provide for selective advantage, for example, providing for biocide resistance, e.g., resistance to antibiotics or heavy metals; complementation, so as to provide prototropy to an auxotrophic host, or the like. Preferably, complementation is employed, so that the modified host may not only be selected, but may also be competitive in the field. One or more markers may be employed in the development of the constructs, as well as for modifying the host. The organisms may be further modified by providing for a competitive advantage against other wild-type microorganisms in the field. For example, genes expressing metal chelating agents, e.g., siderophores, may be introduced into the host along with the structural gene expressing the toxin. In this manner, the enhanced expression of a siderophore may provide for a competitive advantage for the toxin-producing host, so that it may effectively compete with the wild-type microorganisms and stably occupy a niche in the environment.
Where no functional replication system is present, the construct will also include a sequence of at least 50 basepairs (bp), preferably at least about 100 bp, more preferably at least about 1000 bp, and usually not more than about 2000 bp of a sequence homologous with a sequence in the host. In this way, the probability of legitimate recombination is enhanced, so that the gene will be integrated into the host and stably maintained by the host. Desirably, the toxin gene will be in close proximity to the gene providing for complementation as well as the gene providing for the competitive advantage. Therefore, in the event that a toxin gene is lost, the resulting organism will be likely to also lost the complementing gene and/or the gene providing for the competitive advantage, so that it will be unable to compete in the environment with the gene retaining the intact construct.
A large number of transcriptional regulatory regions are available from a wide variety of microorganism hosts, such as bacteria, bacteriophage, cyanobacteria, algae, fungi, and the like. Various transcriptional regulatory regions include the regions associated with the trp gene, lac gene, gal gene, the λL and λR promoters, the tac promoter, the naturally-occurring promoters associated with the δ-endotoxin gene, where functional in the host. See for example, U.S. Pat. Nos. 4,332,898; 4,342,832; and 4,356,270 (each of which is specifically incorporated herein by reference). The termination region may be the termination region normally associated with the transcriptional initiation region or a different transcriptional initiation region, so long as the two regions are compatible and functional in the host.
Where stable episomal maintenance or integration is desired, a plasmid will be employed which has a replication system which is functional in the host. The replication system may be derived from the chromosome, an episomal element normally present in the host or a different host, or a replication system from a virus which is stable in the host. A large number of plasmids are available, such as pBR322, pACYC184, RSF1010, pR01614, and the like. See for example, Olson et al. (1982); Bagdasarian et al. (1981), Baum et al., 1990, and U.S. Pat. Nos. 4,356,270; 4,362,817; 4,371,625, and 5,441,884, each incorporated specifically herein by reference.
The B. thuringiensis gene can be introduced between the transcriptional and translational initiation region and the transcriptional and translational termination region, so as to be under the regulatory control of the initiation region. This construct will be included in a plasmid, which will include at least one replication system, but may include more than one, where one replication system is employed for cloning during the development of the plasmid and the second replication system is necessary for functioning in the ultimate host. In addition, one or more markers may be present, which have been described previously. Where integration is desired, the plasmid will desirably include a sequence homologous with the host genome.
The transformants can be isolated in accordance with conventional ways, usually employing a selection technique, which allows for selection of the desired organism as against unmodified organisms or transferring organisms, when present. The transformants then can be tested for pesticidal activity. If desired, unwanted or ancillary DNA sequences may be selectively removed from the recombinant bacterium by employing site-specific recombination systems, such as those described in U.S. Pat. No. 5,441,884 (specifically incorporated herein by reference).
A B. thuringiensis cry3* gene encoding a crystal protein having one or more mutations in one or more regions of the peptide represents an important aspect of the invention. Preferably, the cry3* gene encodes an amino acid sequence in which one or more amino acid residues have been changed based on the methods disclosed herein, and particularly those changes which have been made for the purpose of altering the insecticidal activity or specificity of the crystal protein.
In accordance with the present invention, nucleic acid sequences include and are not limited to DNA, including and not limited to cDNA and genomic DNA, genes; RNA, including and not limited to mRNA and tRNA; antisense sequences, nucleosides, and suitable nucleic acid sequences such as those set forth in SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:100, or SEQ ID NO:107, and alterations in the nucleic acid sequences including alterations, deletions, mutations, and homologs capable of expressing the B. thuringiensis modified toxins of the present invention.
As such the present invention also concerns DNA segments, that are free from total genomic DNA and that encode the novel synthetically-modified crystal proteins disclosed herein. DNA segments encoding these peptide species may prove to encode proteins, polypeptides, subunits, functional domains, and the like of crystal protein-related or other non-related gene products. In addition these DNA segments may be synthesized entirely in vitro using methods that are well-known to those of skill in the art.
As used herein the term "DNA segment" refers to a DNA molecule that has been isolated free of total genomic DNA of a particular species. Therefore, a DNA segment encoding a crystal protein or peptide refers to a DNA segment that contains crystal protein coding sequences yet is isolated away from, or purified free from, total genomic DNA of the species from which the DNA segment is obtained, which in the instant case is the genome of the Gram-positive bacterial genus, Bacillus, and in particular, the species of Bacillus known as B. thuringiensis. Included within the term "DNA segment", are DNA segments and smaller fragments of such segments, and also recombinant vectors, including, for example, plasmids, cosmids, phagemids, phage, viruses, and the like.
Similarly, a DNA segment comprising an isolated or purified crystal protein-encoding gene refers to a DNA segment which may include in addition to peptide encoding sequences, certain other elements such as, regulatory sequences, isolated substantially away from other naturally occurring genes or protein-encoding sequences. In this respect, the term "gene" is used for simplicity to refer to a functional protein-, polypeptide- or peptide-encoding unit. As will be understood by those in the art, this functional term includes both genomic sequences, operon sequences and smaller engineered gene segments that express, or may be adapted to express, proteins, polypeptides or peptides.
"Isolated substantially away from other coding sequences" means that the gene of interest, in this case, a gene encoding a bacterial crystal protein, forms the significant part of the coding region of the DNA segment, and that the DNA segment does not contain large portions of naturally-occurring coding DNA, such as large chromosomal fragments or other functional genes or operon coding regions. Of course, this refers to the DNA segment as originally isolated, and does not exclude genes, recombinant genes, synthetic linkers, or coding regions later added to the segment by the hand of man.
Particularly preferred DNA sequences are those encoding Cry3Bb.60, Cry3Bb.11221, Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11234, Cry3Bb.11235, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11032, Cry3Bb.11035, Cry3Bb.11036, Cry3Bb.11046, Cry3Bb.11048, Cry3Bb.11051, Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11095 and Cry3Bb.11098 crystal proteins, and in particular cry3Bb* genes such as cry3Bb.60, cry3Bb.11221, cry3Bb.11222, cry3Bb.11223, cry3Bb.11224, cry3Bb.11225, cry3Bb.11226, cry3Bb.11227, cry3Bb.11228, cry3Bb.11229, cry3Bb.11230, cry3Bb.11231, cry3Bb.11232, cry3Bb.11233, cry3Bb.11234, cry3Bb.11235, cry3Bb.11236, cry3Bb.11237, cry3Bb.11238, cry3Bb.11239, cry3Bb.11241, cry3Bb.11242, cry3Bb.11032, cry3Bb.11035, cry3Bb.11036, cry3Bb.11046, cry3Bb.11048, cry3Bb.11051, cry3Bb.11057, cry3Bb.11058, cry3Bb.11081, cry3Bb.11082, cry3Bb.11083 cry3Bb.11084, cry3Bb.11095 and cry3Bb.11098. In particular embodiments, the invention concerns isolated DNA segments and recombinant vectors incorporating DNA sequences that encode a Cry peptide species that includes within its amino acid sequence an amino acid sequence essentially as set forth in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36. SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108.
The term "a sequence essentially as set forth in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108" means that the sequence substantially corresponds to a portion of the sequence of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108, and has relatively few amino acids that are not identical to, or a biologically functional equivalent of, the amino acids of any of these sequences. The term "biologically functional equivalent" is well understood in the art and is further defined in detail herein (e.g., see Illustrative Embodiments).
Accordingly, sequences that have between about 70% and about 75% or between about 75% and about 80%, or more preferably between about 81% and about 90%, or even more preferably between about 91% or 92% or 93% and about 97% or 98% or 99% amino acid sequence identity or functional equivalence to the amino acids of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SFQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102 or SEQ ID NO:108 will be sequences that are "essentially as set forth in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108."
It will also be understood that amino acid and nucleic acid sequences may include additional residues, such as additional N- or C-terminal amino acids or 5' or 3' sequences, and yet still be essentially as set forth in one of the sequences disclosed herein, so long as the sequence meets the criteria set forth above, including the maintenance of biological protein activity where protein expression is concerned. The addition of terminal sequences particularly applies to nucleic acid sequences that may, for example, include various non-coding sequences flanking either of the 5' or 3' portions of the coding region or may include various internal sequences, i.e., introns, which are known to occur within genes.
The nucleic acid segments of the present invention, regardless of the length of the coding sequence itself, may be combined with other DNA sequences, such as promoters, polyadenylation signals, additional restriction enzyme sites, multiple cloning sites, other coding segments, and the like, such that their overall length may vary considerably. It is therefore contemplated that a nucleic acid fragment of almost any length may be employed, with the total length preferably being limited by the ease of preparation and use in the intended recombinant DNA protocol.
For example, nucleic acid fragments may be prepared that include a short contiguous stretch encoding the peptide sequence disclosed in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108, or that are identical to or complementary to DNA sequences which encode the peptide disclosed in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108, and particularly the DNA segments disclosed in SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107.
Highly preferred nucleic acid segments of the present invention comprise one or more cry genes of the invention, or a portion of one or more cry genes of the invention. For certain application, relatively small contiguous nucleic acid sequences are preferable, such as those which are about 14 or 15 or 16 or 17 or 18 or 19, or 20, or 30-50, 51-80, 81-100 or so nucleotides in length. Alternatively, in some embodiments, and particularly those involving preparation of recombinant vectors, transformation of suitable host cells, and preparation of transgenic plant cell, longer nucleic acid segments are preferred, particularly those that include the entire coding region of one or more cry genes. As such, the preferred segments may include those that are up to about 20,000 or so nucleotides in length, or alternatively, shorter sequences such as those about 19,000, about 18,000, about 17,000, about 16,000, about 15,000, about 14,000, about 13,000, about 12,000, 11,000, about 10,000, about 9,000, about 8,000, about 7,000, about 6,000, about 5,000, about 4,500, about 4,000, about 3,500, about 3,000, about 2,500, about 2,000, about 1,500, about 1,000, about 500, or about 200 or so base pairs in length. Of course, these numbers are not intended to be exclusionary of all possible intermediate lengths in the range of from about 20,000 to about 15 nucleotides, as all of these intermediate lengths are also contemplated to be useful, and fall within the scope of the present invention. It will be readily understood that "intermediate lengths", in these contexts, means any length between the quoted ranges, such as 14, 15, 16, 17, 18, 19, 20, etc.; 21, 22, 23, 24, 25, 26, 27, 28, 29, etc.; 30, 31, 32, 33, 34, 35, 36 . . . etc.; 40, 41, 42, 43, 44 . . . etc., 50, 51, 52, 53 . . . etc.; 60, 61, 62, 63 . . . etc., 70, 80, 90, 100, 110, 120, 130 . . . etc.; 200, 210, 220, 230, 240, 250 . . . etc.; including all integers in the entire range from about 14 to about 10,000, including those integers in the ranges 200-500; 500-1,000; 1,000-2,000; 2,000-3,000; 3,000-5,000 and the like.
In a preferred embodiment, the nucleic acid segments comprise a sequence of from about 1800 to about 18,000 base pair in length, and comprise one or more genes which encode a modified Cry3* polypeptide disclosed herein which has increased activity against Coleopteran insect pests.
It will also be understood that this invention is not limited to the particular nucleic acid sequences which encode peptides of the present invention, or which encode the amino acid sequence of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ I) NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108, including the DNA sequences which are particularly disclosed in SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107. Recombinant vectors and isolated DNA segments may therefore variously include the peptide-coding regions themselves, coding regions bearing selected alterations or modifications in the basic coding region, or they may encode larger polypeptides that nevertheless include these peptide-coding regions or may encode biologically functional equivalent proteins or peptides that have variant amino acids sequences.
The DNA segments of the present invention encompass biologically-functional, equivalent peptides. Such sequences may arise as a consequence of codon redundancy and functional equivalency that are known to occur naturally within nucleic acid sequences and the proteins thus encoded. Alternatively, functionally-equivalent proteins or peptides may be created via the application of recombinant DNA technology, in which changes in the protein structure may be engineered, based on considerations of the properties of the amino acids being exchanged. Changes designed by man may be introduced through the application of site-directed mutagenesis techniques, e.g., to introduce improvements to the antigenicity of the protein or to test mutants in order to examine activity at the molecular level.
If desired, one may also prepare fusion proteins and peptides, e.g., where the peptide-coding regions are aligned within the same expression unit with other proteins or peptides having desired functions, such as for purification or immunodetection purposes (e.g., proteins that may be purified by affinity chromatography and enzyme label coding regions, respectively).
Recombinant vectors form further aspects of the present invention. Particularly useful vectors are contemplated to be those vectors in which the coding portion of the DNA segment, whether encoding a full length protein or smaller peptide, is positioned under the control of a promoter. The promoter may be in the form of the promoter that is naturally associated with a gene encoding peptides of the present invention, as may be obtained by isolating the 5' non-coding sequences located upstream of the coding segment or exon, for example, using recombinant cloning and/or PCR™ technology, in connection with the compositions disclosed herein.
In other embodiments, it is contemplated that certain advantages will be gained by positioning the coding DNA segment under the control of a recombinant, or heterologous, promoter. As used herein, a recombinant or heterologous promoter is intended to refer to a promoter that is not normally associated with a DNA segment encoding a crystal protein or peptide in its natural environment. Such promoters may include promoters normally associated with other genes, and/or promoters isolated from any bacterial, viral, eukaryotic, or plant cell. Naturally, it will be important to employ a promoter that effectively directs the expression of the DNA segment in the cell type, organism, or even animal, chosen for expression. The use of promoter and cell type combinations for protein expression is generally known to those of skill in the art of molecular biology, for example, see Sambrook et al., 1989. The promoters employed may be constitutive, or inducible, and can be used under the appropriate conditions to direct high level expression of the introduced DNA segment, such as is advantageous in the large-scale production of recombinant proteins or peptides. Appropriate promoter systems contemplated for use in high-level expression include, but are not limited to, the Pichia expression vector system (Pharmacia LKB Biotechnology).
In connection with expression embodiments to prepare recombinant proteins and peptides, it is contemplated that longer DNA segments will most often be used, with DNA segments encoding the entire peptide sequence being most preferred. However, it will be appreciated that the use of shorter DNA segments to direct the expression of crystal peptides or epitopic core regions, such as may be used to generate anti-crystal protein antibodies, also falls within the scope of the invention. DNA segments that encode peptide antigens from about 8, 9, 10, or 11 or so amino acids, and up to and including those of about 30, 40, or 50 or so amino acids in length, or more preferably, from about 8 to about 30 amino acids in length, or even more preferably, from about 8 to about 20 amino acids in length are contemplated to be particularly useful. Such peptide epitopes may be amino acid sequences which comprise contiguous amino acid sequence from SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, or SEQ ID NO:108.
In one embodiment, the invention provides a transgenic plant having incorporated into its genome a transgene that encodes a contiguous amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6. SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14. SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, SEQ ID NO:102, and SEQ ID NO:108.
A further aspect of the invention is a transgenic plant having incorporated into its genome a cry3Bb* transgene, provided the transgene comprises a nucleic acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, and SEQ ID NO:107. Also disclosed and claimed are progeny of such a transgenic plant, as well as its seed, progeny from such seeds, and seeds arising from the second and subsequent generation plants derived from such a transgenic plant.
The invention also discloses and claims host cells, both native, and genetically engineered, which express the novel cry3Bb* genes to produce Cry3Bb* polypeptides. Preferred examples of bacterial host cells include B. thuringiensis EG11221, EG11222, EG11223, EG11224, EG11225, EG11226, EG11227, EG11228, EG11229, EG11230, EG11231, EG11232, EG11233, EG11234, EG11235, EG11236, EG11237, EG11238, EG11239, EG11241, EG11242, EG11032, EG11035, EG11036, EG11046, EG11048, EG11051, EG11057, EG11058, EG11081, EG11082, EG11083, EG11084, EG11095, and EG11098.
Methods of using such cells to produce Cry3* crystal proteins are also disclosed. Such methods generally involve culturing the host cell (such as B. thuringiensis EG11221, EG11222, EG11223, EG11224, EG11225, EG11226, EG11227, EG11228, EG11229, EG11230, EG11231, EG11232, EG11233, EG11234, EG11235, EG11236, EG11237, EG11238, EG11239, EG11241, EG11242, EG11032, EG11035, EG11036, EG11046, EG11048, EG11051, EG11057, EG11058, EG11081, EG11082, EG11083, EG11084, or EG11095, or EG11098) under conditions effective to produce a Cry3* crystal protein, and obtaining the Cry3* crystal protein from said cell.
In yet another aspect, the present invention provides methods for producing a transgenic plant which expresses a nucleic acid segment encoding the novel recombinant crystal proteins of the present invention. The process of producing transgenic plants is well-known in the art. In general, the method comprises transforming a suitable host cell with one or more DNA segments which contain one or more promoters operatively linked to a coding region that encodes one or more of the disclosed B. thuringiensis crystal proteins. Such a coding region is generally operatively linked to a transcription-terminating region, whereby the promoter is capable of driving the transcription of the coding region in the cell, and hence providing the cell the ability to produce the recombinant protein in vivo. Alternatively, in instances where it is desirable to control, regulate, or decrease the amount of a particular recombinant crystal protein expressed in a particular transgenic cell, the invention also provides for the expression of crystal protein antisense mRNA. The use of antisense mRNA as a means of controlling or decreasing the amount of a given protein of interest in a cell is well-known in the art.
Another aspect of the invention comprises a transgenic plant which express a gene or gene segment encoding one or more of the novel polypeptide compositions disclosed herein. As used herein, the term "transgenic plant" is intended to refer to a plant that has incorporated DNA sequences, including but not limited to genes which are perhaps not normally present, DNA sequences not normally transcribed into RNA or translated into a protein ("expressed"), or any other genes or DNA sequences which one desires to introduce into the non-transformed plant, such as genes which may normally be present in the non-transformed plant but which one desires to either genetically engineer or to have altered expression.
It is contemplated that in some instances the genome of a transgenic plant of the present invention will have been augmented through the stable introduction of one or more Cry3Bb*-encoding transgenes, either native, synthetically modified, or mutated. In some instances, more than one transgene will be incorporated into the genome of the transformed host plant cell. Such is the case when more than one crystal protein-encoding DNA segment is incorporated into the genome of such a plant. In certain situations, it may be desirable to have one, two, three, four, or even more B. thuringiensis crystal proteins (either native or recombinantly-engineered) incorporated and stably expressed in the transformed transgenic plant.
A preferred gene which may be introduced includes, for example, a crystal protein-encoding a DNA sequence from bacterial origin, and particularly one or more of those described herein which are obtained from Bacillus spp. Highly preferred nucleic acid sequences are those obtained from B. thuringiensis, or any of those sequences which have been genetically engineered to decrease or increase the insecticidal activity of the crystal protein in such a transformed host cell.
Means for transforming a plant cell and the preparation of a transgenic cell line are well-known in the art, and are discussed herein. Vectors, plasmids, cosmids, YACs (yeast artificial chromosomes) and DNA segments for use in transforming such cells will, of course, generally comprise either the operons, genes, or gene-derived sequences of the present invention, either native, or synthetically-derived, and particularly those encoding the disclosed crystal proteins. These DNA constructs can further include structures such as promoters, enhancers, polylinkers, or even gene sequences which have positively- or negatively-regulating activity upon the particular genes of interest as desired. The DNA segment or gene may encode either a native or modified crystal protein, which will be expressed in the resultant recombinant cells, and/or which will impart an improved phenotype to the regenerated plant.
Such transgenic plants may be desirable for increasing the insecticidal resistance of a monocotyledonous or dicotyledonous plant, by incorporating into such a plant, a transgenic DNA segment encoding a Cry3Bb* crystal protein which is toxic to coleopteran insects. Particularly preferred plants include grains such as corn, wheat, rye, rice, barley, and oats; legumes such as soybeans; tubers such as potatoes; fiber crops such as flax and cotton; turf and pasture grasses; ornamental plants; shrubs; trees; vegetables, berries, citrus, fruits, cacti, succulents, and other commercially-important crops including garden and houseplants.
In a related aspect, the present invention also encompasses a seed produced by the transformed plant, a progeny from such seed, and a seed produced by the progeny of the original transgenic plant, produced in accordance with the above process. Such progeny and seeds will have one or more crystal protein transgene(s) stably incorporated into its genome, and such progeny plants will inherit the traits afforded by the introduction of a stable transgene in Mendelian fashion. All such transgenic plants having incorporated into their genome transgenic DNA segments encoding one or more Cry3Bb* crystal proteins or polypeptides are aspects of this invention. Particularly preferred transgenes for the practice of the invention include nucleic acid segments comprising one or more cry3Bb* gene(s).
Modification and changes may be made in the structure of the peptides of the present invention and DNA segments which encode them and still obtain a functional molecule that encodes a protein or peptide with desirable characteristics. The following is a discussion based upon changing the amino acids of a protein to create an equivalent, or even an improved, second-generation molecule. In particular embodiments of the invention, mutated crystal proteins are contemplated to be useful for increasing the insecticidal activity of the protein, and consequently increasing the insecticidal activity and/or expression of the recombinant transgene in a plant cell. The amino acid changes may be achieved by changing the codons of the DNA sequence, according to the codons given in Table 4.
TABLE 4
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Amino Acids Codons
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Alanine Ala A GCA GCC GCG GCU
Cysteine Cys C UGC UGU
Aspartic Acid
Asp D GAC GAU
Glutamic Acid
Glu E GAA GAG
Phenylalanine
Phe F UUC UUU
Glycine Gly G GGA GGC GGG GGU
Histidine
His H CAC CAU
Isoleucine
Ile I AUA AUC AUU
Lysine Lys K AAA AAG
Leucine Leu L UUA UUG CUA CUC CUG CUU
Methionine
Met M AUG
Asparagine
Asn N AAC AAU
Proline Pro P CCA CCC CCG CCU
Glutamine
Gln Q CAA CAG
Arginine Arg R AGA AGG CGA CGC CGG CGU
Serine Ser S AGC AGU UCA UCC UCG UCU
Threonine
Thr T ACA ACC ACG ACU
Valine Val V GUA GUC GUG GUU
Tryptophan
Trp W UGG
Tyrosine Tyr Y UAC UAU
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For example, certain amino acids may be substituted for other amino acids in a protein structure without appreciable loss of interactive binding capacity with structures such as, for example, antigen-binding regions of antibodies or binding sites on substrate molecules. Since it is the interactive capacity and nature of a protein that defines that protein's biological functional activity, certain amino acid sequence substitutions can be made in a protein sequence, and, of course, its underlying DNA coding sequence, and nevertheless obtain a protein with like properties. It is thus contemplated by the inventors that various changes may be made in the peptide sequences of the disclosed compositions, or corresponding DNA sequences which encode said peptides without appreciable loss of their biological utility or activity.
In making such changes, the hydropathic index of amino acids may be considered. The importance of the hydropathic amino acid index in conferring interactive biologic function on a protein is generally understood in the art (Kyte and Doolittle, 1982, incorporate herein by reference). It is accepted that the relative hydropathic character of the amino acid contributes to the secondary structure of the resultant protein, which in turn defines the interaction of the protein with other molecules, for example, enzymes, substrates, receptors, DNA, antibodies, antigens, and the like.
Each amino acid has been assigned a hyldropathic index on the basis of their hydrophobicity and charge characteristics (Kyte and Doolittle, 1982), these are: isoleucine (+4.5); valine (+4.2); leucine (+3.8); phenylalanine (+2.8); cysteine/cystine (+2.5); methionine (+1.9); alanine (+1.8); glycine (-0.4); threonine (-0.7); serine (-0.8); tryptophan (-0.9); tyrosine (-1.3); proline (-1.6); histidine (-3.2); glutamate (-3.5); glutamine (-3.5); aspartate (-3.5); asparagine (-3.5); lysine (-3.9); and arginine (-4.5).
It is known in the art that certain amino acids may be substituted by other amino acids having a similar hydropathic index or score and still result in a protein with similar biological activity, i.e., still obtain a biological functionally equivalent protein. In making such changes, the substitution of amino acids whose hydropathic indices are within ±2 is preferred, those which are within ±1 are particularly preferred, and those within ±0.5 are even more particularly preferred.
It is also understood in the art that the substitution of like amino acids can be made effectively on the basis of hydrophilicity. U.S. Pat. No. 4,554,101, specifically incorporated herein by reference, states that the greatest local average hydrophilicity of a protein, as governed by the hydrophilicity of its adjacent amino acids, correlates with a biological property of the protein.
As detailed in U.S. Pat. No. 4,554,101, the following hydrophilicity values have been assigned to amino acid residues: arginine (+3.0); lysine (+3.0); aspartate (+3.0±1); glutamate (+3.0±1); serine (+0.3); asparagine (+0.2); glutamine (+0.2); glycine (0); threonine (-0.4); proline (-0.5±1); alanine (-0.5); histidine (-0.5); cysteine (-1.0); methionine (-1.3); valine (-1.5); leucine (-1.8); isoleucine (-1.8); tyrosine (-2.3); phenylalanine (-2.5); tryptophan (-3.4).
It is understood that an amino acid can be substituted for another having a similar hydrophilicity value and still obtain a biologically equivalent, and in particular, an immunologically equivalent protein. In such changes, the substitution of amino acids whose hydrophilicity values are within ±2 is preferred, those which are within +1 are particularly preferred, and those within ±0.5 are even more particularly preferred.
As outlined above, amino acid substitutions are generally therefore based on the relative similarity of the amino acid side-chain substituents, for example, their hydrophobicity, hydrophilicity, charge, size, and the like. Exemplary substitutions which take various of the foregoing characteristics into consideration are well known to those of skill in the art and include: arginine and lysine; glutamate and aspartate; serine and threonine; glutamine and asparagine; and valine, leucine and isoleucine.
The drawings form part of the present specification and are included to further demonstrate certain aspects of the present invention. The invention may be better understood by reference to one or more of these drawings in combination with the detailed description of specific embodiments presented herein.
FIG. 1. Schematic representation of the monomeric structure of Cry3Bb.
FIG. 2. Stereoscopic view of the monomeric structure of Cry3Bb with associated water molecules (represented by dots).
FIG. 3A. Schematic representation of domain 1 of Cry3Bb
FIG. 3B. Diagram of the positions of the 7 helices that comprise domain 1.
FIG. 4. Domain 1 of Cry3Bb is organized into seven α helices illustrated in FIG. 3A (schematic representation) and FIG. 3B (schematic diagram). The α helices and amino acids residues are shown.
FIG. 5A. Schematic representation of domain 2 of Cry3Bb.
FIG. 5B. Diagram of the positions of the 11 β stands that compose the 3 βsheets of domain 2.
FIG. 6. Domain 2 of Cry3Bb is a collection of three anti-parallel β sheets illustrated in FIG. 5. The amino acids that define these sheets is listed below (α8, amino aids 322-328, also is included in domain 2):
FIG. 7A. Schematic representation of domain 3 of Cry3Bb.
FIG. 7B. Diagram of the positions of the β strands that comprise domain 3.
FIG. 8. Domain 3 (FIG. 7) is a loosely organized collection of β strands and loops; no β sheets are present. The β stands contain the amino acids limited below:
FIG. 9A. A "side" view of the dimeric structure of Cry3Bb. The helical bundles of domains 1 can be seem in the middle of the molecule.
FIG. 9B. A "top" view of the dimeric stricture of Cry3Bb. The helical bundles of domains 1 can be seem in the middle of the molecule.
FIG. 10. A graphic representation of the growth in conductance with time of channels formed by Cry3A and Cry3Bb in planar lipid bilayers. Cry3A forms channels with higher conductances much more rapidly than Cry3Bb.
FIG. 11. A map of pEG1701 which contains the Cry3Bb gene with the cry1F terminator.
FIG. 12. The results of replicated 1-dose assays against SCRW larvae of Cry3Bb proteins altered in the 1B2,3 region.
FIG. 13. The results of replicated, 1-dose assays against SCRW larvae of Cry3Bb proteins altered in the 1B6, 7 region.
FIG. 14. The results of replicated, 1-dose screens against SCRW larvae of Cry3Bb proteins altered in the 1B10,11 region.
FIG. 15. Single channel recordings of channels formed by Cry3Bb.11230 and WT Cry3Bb in planar lipid bilayers. Cry3Bb.11230 forms channels with well resolved open and closed states while Cry3Bb rarely does.
FIG. 16. Single channel recordings of channels formed by Cry3Bb and Cry3Bb.60, a truzncated form of Cry3Bb. Cry3Bb.60 forms channels more quickly than Cry3Bb and, unlike Cry3Bb, produces channels with well resolved open and closed states.
FIG. 17A. Sequence alignment of the amino acid sequence of Cry3C (SEQ ID NO:109), Cry3Bb2 (SEQ ID NO:110), Cry3Bb (SEQ ID NO:111), Cry3Ba (SEQ ID NO:112), and Cry3A (SEQ ID NO:113).
FIG. 17B. Shown is a continuation of alignment of the amino acid sequence of Cry3C (SEQ ID NO:109), Cry3Bb2 (SEQ ID NO:110), Cry3Bb (SEQ ID NO:111), Cry3Ba (SEQ ID NO:112), and Cry3A (SEQ ID NO:113) shown in FIG. 17A.
FIG. 17C. Shown is a continuation of alignment of the amino acid sequence of Cry3C (SEQ ID NO:109), Cry3Bb2 (SEQ ID NO:110), Cry3Bb (SEQ ID NO:111), Cry3Ba (SEQ ID NO:112), and Cry3A (SEQ ID NO:113) shown in FIG. 17A.
The invention defines new B. thuringiensis (Bt) insecticidal δ-endotoxin proteins and the biochemical and biophysical strategies used to design the new proteins. Delta-endodtoxins are a class of insecticdal proteins produced by B. thuringiensis that form cation-selective channels in planar lipid bilayers (English and Slatin, 1992). The new δ-endotoxins are based on the parent structure of the coleopteran-active, δ-endotoxin Cry3Bb. Like other members of the coleopteran-active class of δ-endotoxins, including Cry3A and Cry3B, Cry3Bb exhibits excellent insecticidal activity against the Colorado Potato Beetle (Leptinotarsa decemlineata). However, unlike Cry3A and Cry3B, Cry3Bb is also active against the southern corn rootworm or SCRW (Diabriotica undecimpunctata howardi Barber) and the western corn rootworm or WCRW (Diabrotica virgifera virgifera LeConte). The new insecticidal proteins described herein were specifically designed to improve the biological activity of the parent Cry3Bb protein. In addition, the design strategies themselves are novel inventions capable of being applied to and improving B. thuringiensis δ-endotoxins in general. B. thuringiensis δ-endotoxins are also members of a larger class of bacterial toxins that form ion channels (see English and Slatin 1992, for a review). The inventors, therefore, believe that these design strategies can also be applied to any biologically active, channel-forming protein to improve its biological properties.
The designed Cry3Bb proteins were engineered using one or more of the following strategies including (1) identification and alteration of protease-sensitive sites and proteolytic processing; (2) analysis and manipulation of bound water; (3) manipulation of hydrogen bonds around mobile regions; (4) loop analysis and loop redesign around flexible helices; (5) loop design around β strands and β sheets; (6) identification and redesign of complex electrostatic surfaces; (7) identification and removal of metal binding sites; (8) alteration of quaternary structure; (9) identification and design of structural residues; and (10) combinations of any and all sites defined by strategies 1-9. These design strategies permit the identification and redesign of specific sites on Cry3Bb, ultimately creating new proteins with improved insecticidal activities. These new proteins are designated Cry3Bb designed proteins and are named Cry3Bb followed by a period and a suffix (e.g, Cry3Bb.60, Cry3Bb.11231). The new proteins are listed in Table 2 along with the specific sites on the molecule that were modified, the amino-acid sequence changes at those sites that improve biological activity, the improved insecticidal activities and the design method used to identify that specific site.
Mutagenesis studies with cry genes have failed to identify a significant number of mutant crystal proteins which have improved broad-spectrum insecticidal activity, that is, with improved toxicity towards a range of insect pest species. Since agricultural crops are typically threatened by more than one insect pest species at any given time, desirable mutant crystal proteins are preferably those that exhibit improvements in toxicity towards multiple insect pest species. Previous failures to identify such mutants may be attributed to the choice of sites targeted for mutagenesis. For example, with respect to the related protein, Cry1C, sites within domain 2 and domain 3 have been the principal targets of mutagenesis efforts, primarily because these domains are believed to be important for receptor binding and in determining insecticidal specificity (Aronson et al., 1995; Chen et al. 1993; de Maagd et al., 1996; Lee et al., 1992; Lee et al., 1995; Lu et al., 1994; Smedley and Ellar, 1996; Smith and Ellar, 1994; Rajamohan et al., 1995; Rajamohan et al., 1996) In contrast, the present inventors reasoned that the toxicity of Cry3 proteins, and specifically the toxicity of the Cry3Bb protein, may be improved against a broader array of target pests by targeting regions involved in ion channel function rather than regions of the molecule directly involved in receptor interactions, namely domains 2 and 3. Accordingly, the inventors opted to target regions within domain 1 cf Cry3Bb for mutagenesis for the purpose of isolating Cry3Bb mutants with improved broad spectrum toxicity. Indeed, in the present sent invention, Cry3Bb mutants are described that show improved toxicity towards several coleopteran pests.
At least one, and probably more than one, α helix of domain 1 is involved in the formation of ion channels and pores within the insect midgut epithelium (Gazit and Shai, 1993; Gazit and Shai, 1995). Rather than target for mutagenesis the sequences encoding the α helices of domain 1 as others have (Wu and Aronson, 1992; Aronson et al., 1995; Chen et al., 1995), the present inventors opted to target exclusively sequences encoding amino acid residues adjacent to or lying within the predicted loop regions of Cry3Bb that separate these α helices. Amino acid residues within these loop regions or amino acid residues capping the end of an α helix and lying adjacent to these loop regions may affect the spatial relationships among these α helices. Consequently, the substitution of these amino acid residues may result in subtle changes in tertiary structure, or even quaternary structure, that positively impact the function of the ion channel. Amino acid residues in the loop regions of domain 1 are exposed to the solvent and thus are available for various molecular interactions. Altering these amino acids could result in greater stability of the protein by eliminating or occluding protease-sensitive sites. Amino acid substitutions that change the surface charge of domain 1 could alter ion channel efficiency or alter interactions with the brush border membrane or with other portions of the toxin molecule allowing binding or insertion to be more effective.
According to this invention, base substitutions are made in the underlying cry3Bb nucleic acid residues in order to change particular codons of the corresponding polypeptides, and particularly, in those loop regions between α-helices. The insecticidal activity of a crystal protein ultimately dictates the level of crystal protein required for effective insect control. The potency of an insecticidal protein should be maximized as much as possible in order to provide for its economic and efficient utilization in the field. The increased potency of an insecticidal protein in a bioinsecticide formulation would be expected to improve the field performance of the bioinsecticide product. Alternatively, increased potency of an insecticidal protein in a bioinsecticide formulation may promote use of reduced amounts of bioinsecticide per unit area of treated crop, thereby allowing for more cost-effective use of the bioinsecticide product. When expressed in planta, the production of crystal proteins with improved insecticidal activity can be expected to improve plant resistance to susceptible insect pests.
The B. thuringiensis strains described herein may be cultured using standard known media and fermentation techniques. Upon completion of the fermentation cycle, the bacteria may be harvested by first separating the B. thuringiensis spores and crystals from the fermentation broth by means well known in the art. The recovered B. thuringiensis spores and crystals can be formulated into a wettable powder, a liquid concentrate, granules or other formulations by the addition of surfactants, dispersants, inert carriers and other components to facilitate handling and application for particular target pests. The formulation and applition procedures are all well known in the art.
The nucleotide sequences of the subject invention can be introduced into a wide variety of microbial hosts. Expression of the toxin gene results, directly or indirectly, in the intracellular production and maintenance of the pesticide. With suitable hosts, e.g., Pseudomonas, the microbes can be applied to the sites of coleopteran insects where they will proliferate and be ingested by the insects. The result is a control of the unwanted insects. Alternatively, the microbe hosting the toxin gene can be treated under conditions that prolong the activity of the toxin produced in the cell. The treated cell then can be applied to the environment of target pest(s). The resulting product retains the toxicity of the B. thuringiensis toxin.
Suitable host cells, where the pesticide-containing cells will be treated to prolong the activity of the toxin in the cell when the then treated cell is applied to the environment of target pest(s), may include either prokaryotes or eukaryotes, normally being limited to those cells which do not produce substances toxic to higher organisms, such as mammals. However, organisms which produce substances toxic to higher organisms could be used, where the toxin is unstable or the level of application sufficiently low as to avoid any possibility or toxicity to a mammalian host. As hosts, of particular interest will be the prokaryotes and the lower eukaryotes, such as fungi. Illustrative prokaryotes, both Gram-negative and Gram-positive, include Enterobacteriaceae, such as Escherichia, Erwinia, Shigella, Salmonella, and Proteus; Bacillaceae; Rhizobiceae, such as Rhizobium, Spirillaceae, such as photobacterium, Zymomonas, Serratia, Aeromonas, Vibrio, Desulfovibrio, Spirillum, Lactobacillaceae; Pseudomonadaceae, such as Pseudomonas and Acetobacter, Azotobacteraceae, Actinomycetales, and Nitrobacteraceae. Among eukaryotes are fungi, such as Phycomycetes and Ascomycetes, which includes yeast, such as Saccaromyces and Schizosaccharomyces; and Basidiomycetes yeast, such as Rhodlotorula, Aureobasidium, Sporobolomyces, and the like.
Characteristics of particular interest in selecting a host cell for purposes of production include ease of introducing the B. thuringiensis gene into the host, availability of expression systems, efficiency of expression, stability of the pesticide in the host, and the presence of auxiliary genetic capabilities. Characteristics of interest for use as a pesticide microcapsule include protective qualities for the pesticide, such as thick cell walls, pigmentation, and intracellular packaging or formation of inclusion bodies; leaf affinity; lack of mammalian toxicity; attractiveness to pests for ingestion; ease of killing and fixing without damage to the toxin; and the like. Other considerations include ease of formulation and handling, economics, storage stability, and the like.
Host organisms of particular interest include yeast, such as Rhodotorula sp., Aureobasidium sp., Saccharomyces sp., and Sporolbolomyces sp., phylloplane organisms such as Pseudomonas sp., Erwinia sp. and Flavobacterium sp.; or such other organisms as Escherichia, Lactobacillus sp., Bacillus sp., Streptoinivces sp., and the like. Specific organisms include Pseudomonas aeruginosa, Pseudomonas fluorescens, Saccharomyces cerevisiae; B. thuringiensis, Escherichia coli, B. subtilis, B. megaterium, B. cereus, Streptomyces lividans and the like.
Treatment of the microbial cell, e.g., a microbe containing the B. thuringiensis toxin gene, can be by chemical or physical means, or by a combination of chemical and/or physical means, so long as the technique does not deleteriously affect the properties of the toxin, nor diminish the cellular capability in protecting the toxin. Examples of chemical reagents are halogenating agents, particularly halogens of atomic no. 17-80. More particularly, iodine can be used under mild conditions and for sufficient time to achieve the desired results. Other suitable techniques include treatment with aldehydes, such as formaldehyde and glutaraldehye; anti-infectives, such as zephiran chloride and cetylpyridinium chloride; alcohols, such as isopropyl and ethanol; various histologic fixatives, such as Lugol's iodine, Bouin's fixative, and Helly's fixatives, (see e.g., Humason, 1967); or a combination of physical (heat) and chemical agents that preserve and prolong the activity of the toxin produced in the cell when the cell is administered to the host animal. Examples of physical means are short wavelength radiation such as γ-radiation and X-radiation, freezing, UV irradiation, lyophilization, and the like. The cells employed will usually be intact and be substantially in the proliferative form when treated, rather than in a spore form, although in some instances pores may be employed.
Where the B. thuringiensis toxin gene is introduced via a suitable vector into a microbial host, and said host is applied to the environment in a living state, it is essential that certain host microbes be used. Microorganism hosts are selected which are known to occupy the "phytosphere" (phylloplane, phyllosphere, rhizosphere, and/or rhizoplane) of one or more crops of interest. These microorganisms are selected so as to be capable of successfully competing in the particular environment (crop and other insect habitats) with the wild-type microorganisms, provide for stable maintenance and expression of the gene expressing the polypeptide pesticide, and, desirably, provide for improved protection of the pesticide from environmental degradation and inactivation.
A large number of microorganisms are known to inhabit the phylloplane (the surface of the plant leaves) and/or the rhizosphere (the soil surrounding plant roots) of a wide variety of important crops. These microorganisms include bacteria, algae, and fungi. Of particular interest are microorganisms, such as bacteria, e.g., genera Bacillus (including the species and subspecies B. thuringiensis kurstaki HD-1, B. thuringiensis kurstaki HD-73, B. thuringiensis sotto, B. thuringiensis berliner, B. thuringiensis thuringiensis, B. thuringiensis tolworthi, B. thuringiensis dendrolimus, B. thuringiensis alesti, B. thuringiensis galleriae, B. thuringiensis aizawai, B. thuringiensis subtoxicus, B. thuringiensis entomocidus, B. thuringiensis jenebrionis and B. thuringiensis san diego); Pseudomonas, Erwinia, Serratia, Klebsiella, Zanthomonas, Streptomyces, Rhizobium, Rhodopseudomonas, Methylophilius, Agrobacterium, Acetobacter, Lactobacillus, Arthrobacter, Azotobacter, Leuconostoc, and Alcaligenes; fungi, particularly yeast, e.g., genera Saccharomyces, Cryptococcus, Kluyveromyces, Sporobolomyces, Rhodotorula, and Aureobasidium. Of particular interest are such phytosphere bacterial species as Pseudomonas syringae, Pseudomonas fluorescens, Serratia marcescens, Acetobacter xylinum, Agrobacterium tumefaciens, Rhodobacter sphaeroides, Xanthomonas campestris, Rhizobium melioti, Alcaligenes eutrophus, and Azotobacter vinlandii; and phytosphere yeast species such as Rhodotorula rubra, R. glutinis, R. marina, R. aurantiaca, Cryptococcus albidus, C. diffluens, C. laurentii, Saccharomyces rosei, S. pretoriensis, S. cerevisiae, Sporobolomyces roseus, S. odorus, Kluyveromyces veronae, and Aureobasidium pollulans.
In accordance with the present invention, nucleic acid sequences include and are not limited to DNA (including and not limited to genomic or extragenomic DNA), genes, RNA (including and not limited to mRNA and tRNA), nucleosides, and suitable nucleic acid segments either obtained from native sources, chemically synthesized, modified, or otherwise prepared by the hand of man. The following words and phrases have the meanings set forth below.
A, an: In accordance with long standing patent law convention, the words "a" and "an" when used in this application, including the claims, denotes "one or more".
Broad-spectrum: Refers to a wide range of insect species.
Broad-spectrum activity: The toxicity towards a wide range of insect species.
Expression: The combination of intracellular processes, including transcription and translation undergone by a coding DNA molecule such as a structural gene to produce a polypeptide.
Insecticidal activity: The toxicity towards insects.
Insecticidal specificity: The toxicity exhibited by a crystal protein or proteins, microbe or plant, towards multiple insect species.
Intraorder specificity: The toxicity of a particular crystal protein towards insect species within an Order of insects (e.g., Order Coleoptera).
Interorder specificity: The toxicity of a particular crystal protein towards insect species of different Orders (e.g., Orders Coleoptera and Diptera).
LC50 : The lethal concentration of crystal protein that causes 50% mortality of the insects treated.
LC95 : The lethal concentration of crystal protein that causes 95% mortality of the insects treated.
Promoter: A recognition site on a DNA sequence or group of DNA sequences that provide an expression control element for a structural gene and to which RNA polymerase specifically binds and initiates RNA synthesis (transcription) of that gene.
Regeneration: The process of growing a plant from a plant cell (e.g., plant protoplast or explant).
Structural gene: A gene that is expressed to produce a polypeptide.
Transformation: A process of introducing an exogenous DNA sequence (e.g., a vector, a recombinant DNA molecule) into a cell or protoplast in which that exogenous DNA is incorporated into a chromosome or is capable of autonomous replication.
Transformed cell: A cell whose DNA has been altered by the introduction of an exogenous DNA molecule into that cell.
Transgenic cell: Any cell derived or regenerated from a transformed cell or derived from a transgenic cell. Exemplary transgenic cells include plant calli derived from a transformed plant cell and particular cells such as leaf, root, stem, e.g., somatic cells, or reproductive (germ) cells obtained from a transgenic plant.
Transgenic plant: A plant or progeny thereof derived from a transformed plant cell or protoplast, wherein the plant DNA contain, an introduced exogenous DNA molecule not originally present in a native, non-transgenic plant of the same strain. The terms "transgenic plant" and "transformed plant" have sometimes been used in the art as synonymous terms to define a plant whose DNA contains an exogenous DNA molecule. However, it is thought more scientifically correct to refer to a regenerated plant or callus obtained from a transformed plant cell or protoplast as being a transgenic plant, and that usage will be followed herein.
Vector: A DNA molecule capable of replication in a host cell and/or to which another DNA segment can be operatively linked so as to bring about replication of the attached segment. A plasmid is an exemplary vector.
As used herein, the designations "CryIII" and "Cry3" are synonymous, as are the designations "CryIIIB2" and "Cry3Bb." Likewise, the inventors have utilized the generic term Cry3Bb* to denote any and all Cry3Bb variants which comprise amino acid sequences modified in the protein. Similarly, cry3Bb* is mean to denote any and all nucleic acid segments and/or genes which encode a Cry3Bb* protein, etc.
Once the structure of the desired peptide to be mutagenized has been analyzed using one or more of the design strategies disclosed herein, it will be desirable to introduce one or more mutations into either the protein or, alternatively, into the DNA sequence encoding the protein for the purpose of producing a mutated protein with altered bioinsecticidal properties.
To that end, the present invention encompasses both site-specific mutagenesis methods and random mutagenesis of a nucleic acid segment encoding a crystal protein in the manner described herein. In particular, methods are disclosed for the mutagenesis of nucleic acid segments encoding the amino acid sequences using one or more of the design strategies described herein. Using the assay methods described herein, one may then identify mutants arising from these procedures which have improved insecticidal properties or altered specificity, either intraorder or interorder.
The means for mutagenizing a DNA segment encoding a crystal protein are well-known to those of skill in the art. Modifications may be made by random, or site-specific mutagenesis procedures. The nucleic acid may be modified by altering its structure through the addition or deletion of one or more nucleotides from the sequence.
Mutagenesis may be performed in accordance with any of the techniques known in the art such as and not limited to synthesizing an oligonucleotide having one or more mutations within the sequence of a particular crystal protein. A "suitable host" is any host which will express Cry3Bb, such as and not limited to B. thuringiensis and E. coli. Screening for insecticidal activity, in the case of Cry3Bb includes and is not limited to coleopteran-toxic activity which may be screened four by techniques known in the art.
In particular, site-specific mutagenesis is a technique useful in the preparation of individual peptides, or biologically functional equivalent proteins or peptides, through specific mutagenesis of the underlying DNA. The technique further provides a ready ability to prepare and test sequence variants, for example, incorporating one or more of the foregoing considerations, by introducing one or more nucleotide sequence changes into the DNA. Site-specific mutagenesis allows the production of mutants through the use of specific oligonucleotide sequences which encode the DNA sequence of the desired mutation, as well as a sufficient number of adjacent nucleotides, to provide a primer sequence of sufficient size and sequence complexity to form a stable duplex on both sides of the deletion junction being traversed. Typically, a primer of about 17 to about 75 nucleotides or more in length is preferred, with about 10 to about 25 or more residues on both sides of the junction of the sequence being altered.
In general, the technique of site-specific mutagenesis is well known in the art, as exemplified by various publications. As will be appreciated, the technique typically employs a phage vector which exists in both a single stranded and double stranded form. Typical vectors useful in site-directed mutagenesis include vectors such as the M13 phage. These phage are readily commercially available and their use is generally well known to those skilled in the art. Double stranded plasmids art also routinely employed in site directed mutagenesis which eliminates the step of transferring the gene of interest from a plasmid to a phage.
In general, site-directed mutagenesis in accordance herewith is performed by first obtaining a single-stranded vector or melting apart of two strands of a double stranded vector which includes within its sequence a DNA sequence which encodes the desired peptide. An oligonucleotide primer bearing the desired mutated sequence is prepared, generally synthetically. This primer is then annealed with the single-stranded vector, and subjected to DNA polymerizing enzymes such as E. coli polymerase I Klenow fragment, in order to complete the synthesis of the mutation-bearing strand. This, a heteroduplex is formed wherein one strand encodes the original non-mutated sequence and the second strand bears the desired mutation. This heteroduplex vector is then used to transform or transfect appropriate cells, such as E. coli cells. and clones are selected which include recombinant vectors bearing the mutated sequence arrangement. A genetic selection scheme was devised by Kunkel et al. (1987) to enrich for clones incorporating the mutagenic oligonucleotide. Alternatively, the use of PCR™ with commercially available thermostable enzymes such as Taq polymerase may be used to incorporate a mutagenic oligonucleotide primer into an amplified DNA fragment that can then be cloned into an appropriate cloning or expression vector. The PCR™-mediated mutagenesis procedures of Tomic et al. (1990) and Upender et al. (1995) provide two examples of such protocols. A PCR™ employing a thermostable ligase in addition to a thermostable polymerase may also be used to incorporate a phosphorylated mutagenic oilgonucleotide into an amplified DNA fragment that may then be cloned into an appropriate cloning or expression vector. The mutagenesis procedure described by Michael (1994) provides an example of one such protocol.
The preparation of sequence variants of the selected peptide-encoding DNA segments using site-directed mutagenesis is provided as a means of producing potentially useful species and is not meant to be limiting as there are other ways in which sequence variants of peptides and the DNA sequences encoding them may be obtained. For example, recombinant vectors encoding the desired peptide sequence may be treated with mutagenic agents, such as hydroxylamine, to obtain sequence variants.
As used herein, the term "oligonucleotide directed mutagenesis procedure" refers to template-dependent processes and vector-mediated propagation which result in an increase in the concentration of a specific nucleic acid molecule relative to its initial concentration, or in an increase in the concentration of a detectable signal, such as amplification. As used herein, the term "oligonucleotide directed mutagenesis procedure" is intended to refer to a process that involves the template-dependent extension of a primer molecule. The term template dependent process refers to nucleic acid synthesis of an RNA or a DNA molecule wherein the sequence of the newly synthesized strand of nucleic acid is dictated by the well-known rules of complementary base pairing (see, for example, Watson, 1987). Typically, vector mediated methodologies involve the introduction of the nucleic acid fragment into a DNA or RNA vector, the clonal amplification of the vector, and the recovery of the amplified nucleic acid fragment. Examples of such methodologies are provided by U. S. Pat. No. 4,237,224, specifically incorporated herein by reference in its entirety.
A number of template dependent processes are available to amplify the target sequences of interest present in a sample. One of the best known amplification methods is the polymerase chain reaction (PCR™) which is described in detail in U.S. Pat. Nos. 4,683,195, 4,683,202 and 4,800,159 (each of which is specifically incorporated herein by reference in its entirety). Briefly, in PCR™, two primer sequences are prepared which are complementary to regions on opposite complementary strands of the target sequence. An excess of deoxynucleoside triphosphates are added to a reaction mixture along with a DNA polymerase (e.g., Taq polymerase). If the target sequence is present in a sample, the primers will bind to the target and the polymerase will cause the primers to be extended along the target sequence by adding on nucleotides. By raising and lowering the temperature of the reaction mixture, the extended primers will dissociate from the target to form reaction products, excess primers will bind to the target and to the reaction products and the process is repeated. Preferably a reverse transcriptase PCR™ amplification procedure may be performed in order to quantify the amount of mRNA amplified. Polymerase chain reaction methodologies are well known in the art.
Another method for amplification is the ligase chain reaction (referred to as LCR), disclosed in Eur. Pat. Appl. Publ. No. 320,308, incorporated herein by reference in its entirety. In LCR, two complementary probe pairs are prepared, and in the presence of the target sequence, each pair will bind to opposite complementary strands of the target such that they abut. In the presence of a ligase, the two probe pairs will link to form a single unit. By temperature cycling, as in PCR™, bound ligated units dissociate from the target and then serve as "target sequences" for ligation of excess probe pairs. U.S. Pat. No. 4,883,750, specifically incorporated herein by reference in its entirety, describes an alternative method of amplification similar to LCR for binding probe pairs to a target sequence.
Qbeta Replicase™, described in Intl. Pat. Appl. Publ. No. PCT/US87/00880, incorporated herein by reference in its entirety, may also be used as still another amplification method in the present invention. In this method, a replicative sequence of RNA which has a region complementary to that of a target is added to a sample in the presence of an RNA polymerase. The polymerase will copy the replicative sequence which can then be detected.
An isothermal amplification method, in which restriction endonucleases and ligases are used to achieve the amplification of target molecules that contain nucleotide 5'-[α-thio]triphosphates in one strand of a restriction site (Walker et al., 1992, incorporated herein by reference in its entirety), may also be useful in the amplification of nucleic acids in the present invention.
Strand Displacement Amplification (SDA) is another method of carrying out isothermal amplification of nucleic acids which involves multiple rounds of strand displacement and synthesis, i.e., nick translation. A similar method, called Repair Chain Reaction (RCR) is another method of amplification which may be useful in the present invention and is involves annealing several probes throughout a region targeted for amplification, followed by a repair reaction in which only two of the four bases are present. The other two bases can be added as biotinylated derivatives for easy detection. A similar approach is used in SDA
Sequences can also be detected using a cyclic probe reaction (CPR). In CPR, a probe having 3' and 5' end sequences of non-Cry-specific DNA and an internal sequence of a Cry-specific RNA is hybridized to DNA which is present in a sample. Upon hybridization, the reaction is treated with RNaseH, and the products of the probe identified as distinctive products generating a signal which are released after digestion. The original template is annealed to another cycling probe and the reaction is repeated. Thus, CPR involves amplifying a signal generated by hybridization of a probe to a cry-specific expressed nucleic acid.
Still other amplification methods described in Great Britain Pat. Appl. No. 2 202 328, and in Intl. Pat. Appl. Publ. No. PCT/US89/03 025, each of which is incorporated herein by reference in its entirety, may be used in accordance with the present invention. In the former application, "modified" primers are used in a PCR™ like, template and enzyme dependent synthesis. The primers may be modified by labeling with a capture moiety (e.g., biotin) and/or a detector moiety (e.g., enzyme). In the latter application, an excess of labeled probes are added to a sample. In the presence of the target sequence, the probe binds and is cleaved catalytically. After cleavage, the target sequence is released intact to be bound by excess probe. Cleavage of the labeled probe signals the presence of the target sequence.
Other nucleic acid amplification procedures include transcription-based amplification systems (TAS) (Kwoh et al., 1989; Intl. Pat. Appl. Publ. No. WO 88/10315, incorporated herein by reference in its entirety), including nucleic acid sequence based amplification (NASBA) and 3SR. In NASBA, the nucleic acids can be prepared for amplification by standard phenol/chloroform extraction, heat denaturation of a sample, treatment with lysis buffer and minispin columns for isolation of DNA and RNA or guanidinium chloride extraction of RNA. These amplification techniques involve annealing a primer which has crystal protein-specific sequences. Following polymerization, DNA/RNA hybrids are digested with RNase H while double stranded DNA molecules are heat denatured again. In either case the single stranded DNA is made fully double stranded by addition of second crystal protein-specific primer, followed by polymerization. The double stranded DNA molecules are then multiply transcribed by a polymerase such as T7 or SP6. In an isothermal cyclic reaction, the RNAs are reverse transcribed into double stranded DNA, and transcribed once against with a polymerase such as T7 or SP6. The resulting products, whether truncated or complete, indicate crystal protein-specific sequences.
Eur. Pat. Appl. Publ. No. 329,822, incorporated herein by reference in its entirety, disclose a nucleic acid amplification process involving cyclically synthesizing single-stranded RNA ("ssRNA"), ssDNA, and double-stranded DNA (dsDNA), which may be used in accordance with the present invention. The ssRNA is a first template for a first primer oligonucleotide, which is elongated by reverse transcriptase (RNA-dependent DNA polymerase). The RNA is then removed from resulting DNA:RNA duplex by the action of ribonuclease H (RNase H, an RNase specific for RNA in a duplex with either DNA or RNA). The resultant ssDNA is a second template for a second primer, which also includes the sequences of an RNA polymerase promoter (exemplified by T7 RNA polymerase) 5' to its homology to its template. This primer is then extended by DNA polymerase (exemplified by the large "Klenow" fragment of E. coli DNA polymerase I), resulting as a double-stranded DNA ("dsDNA") molecule, having a sequence identical to that of the original RNA between the primers and having additionally, at one end, a promoter sequence. This promoter sequence can be used by the appropriate RNA polymerase to make many RNA copies of the DNA. These copies can then re-enter the cycle leading to very swift amplification. With proper choice of enzymes, this amplification can be done isothermally without addition of enzymes at each cycle. Because of the cyclical nature of this process, the starting sequence can be chosen to be in the form of either DNA or RNA.
Intl. Pat. Appl. Publ. No. WO 89/06700, incorporated herein by reference in its entirety, disclose a nucleic acid sequence amplification scheme based on the hybridization of a promoter/primer sequence to a target single-stranded DNA ("ssDNA") followed by transcription of many RNA copies of the sequence. This scheme is not cyclic; i.e., new templates are not produced from resultant RNA transcripts. Other amplification methods include "RACE" (Frohman, 1990), and "one-sided PCR™" (Ohara, 1989) which are well-known to those of skill in the art.
Methods based on ligation of two (or more) oligonucleotides in the presence of nucleic acid having the sequence of the resulting "di-oligonucleotide", thereby amplifying the di-oligonucleotide (Wu and Dean, 1996, incorporated herein by reference in its entirety), may also be used in the amplification of DNA sequences of the present invention.
In certain embodiments, one may desired to prepare one or more phage resistant variants of the B. thuringiensis mutants prepared by the methods described herein. To do so, an aliquot of a phage lysate is spread onto nutrient agar and allowed to dry. An aliquot of the phage sensitive bacterial strain is then plated directly over the dried lysate and allowed to dry. The plates are incubated at 30° C. The plates are incubated for 2 days and, at that time, numerous colonies could be seen growing on the agar. Some of these colonies are picked and subcultured onto nutrient agar plates. These apparent resistant cultures are tested for resistance by cross streaking with the phage lysate. A line of the phage lysate is streaked on the plate and allowed to dry. The presumptive resistant cultures are then streaked across the phage line. Resistant bacterial cultures show no lysis anywhere in the streak across the phage line after overnight incubation at 30° C. The resistance to phage is then reconfirmed by plating a lawn of the resistant culture onto a nutrient agar plate. The sensitive strain is also plated in the same manner to serve as the positive control. After drying, a drop of the phage lysate is plated in the center of the plate and allowed to dry. Resistant cultures showed no lysis in the area where the phage lysate has been placed after incubation at 30° C. for 24 hours.
Order Coleoptera comprises numerous beetle species including ground beetles, reticulated beetles, skin and larder beetles, long-horned beetles, leaf beetles, weevils, bark beetles, ladybird beetles, soldier beetles, stag beetles, water scavenger beetles, and a host of other beetles. A brief taxonomy of the Order is given at the website http://www.ncbi.nlm.nih.gov/Taxonomy/tax.html.
Particularly important among the Coleoptera are the agricultural pests included within the infraorders Chrysomeliformia and Cucujiformia. Members of the infraorder Chrysomeliformia, including the leaf beetles (Chrysomelidae) and the weevils (Curculionidae), are particularly problematic to agriculture, and are responsible for a variety of insect damage to crops and plants. The infraorder Cucujiformia includes the families Coccinellidae, Cucujidae, Lagridae, Meloidae, Rhipiphoridae, and Tenebrionidae. Within this infraorder, members of the family Chrysomelidae (which includes the genera Exema, Chrysomela, Oreina, Chrysolina, Leptinotarsa, Gonioctena, Oulema, Monozia, Ophraella, Cerotoma, Diabrotica, and Lachnaia), are well-known for their potential to destroy agricultural crops.
As the toxins of the present invention have been shown to be effective in combatting a variety of members of the order Coleoptera, the inventors contemplate that the insects of many Coleopteran genera may be controlled or eradicated using the polypeptide compositions described herein. Likewise, the methods described herein for generating modified polypeptides having enhanced insect specificity may also be useful in extending the range of the insecticidal activity of the modified polypeptides to other insect species within, and outside of, the Order Coleoptera.
As such, the inventors contemplate that the crystal protein compositions disclosed herein will find particular utility as insecticides for topical and/or systemic application to field crops, including but not limited to rice, wheat, alfalfa, corn (maize), soybeans, tobacco, potato, barley, canola (rapeseed), sugarbeet, sugarcane, flax, rye, oats, cotton, sunflower; grasses, such as pasture and turf grasses; fruits, citrus, nuts, trees, shrubs and vegetables; as well as ornamental plants, cacti, succulents, and the like.
Disclosed and claimed is a composition comprising an insecticidally-effective amount of a Cry3Bb* crystal protein composition. The composition preferably comprises the amino acid sequence of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48 SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, or SEQ ID NO:108 or biologically-functional equivalents thereof.
The insecticide composition may also comprise a Cry3Bb* crystal protein that is encoded by a nucleic acid sequence having the sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, or SEQ ID NO:108, or, alternatively, a nucleic acid sequence which hybridizes to the nucleic acid sequence of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, or SEQ ID NO:107 under conditions of moderate stringency.
The insecticidal compositions may comprise one or more B. thuringiensis cell types, or one or more cultures of such cells, or, alternatively, a mixture of one or more B. thuringiensis cells which express one or more of the novel crystal proteins of the invention in combination with another insecticidal composition. In certain aspects it may be desirable to prepare compositions which contain a plurality of crystal proteins, either native or modified, for treatment of one or more types of susceptible insects. The B. thuringiensis cells of the invention can be treated prior to formulation to prolong the insecticidal activity when the cells are applied to the environment of the target insect(s) Such treatment can be by chemical or physical means, or by a combination of chemical and/or physical means, so long as the technique does not deleteriously affect the properties of the insecticide, nor diminish the cellular capability in protecting the insecticide. Examples of chemical reagents are halogenerating agents, particularly halogens of atomic no. 17-80 More particularly, iodine can be used under mild conditions and for sufficient time to achieve the desired results. Other suitable techniques include treatment with aldehydes, such as formaldehyde and glutaraldehyde; anti-infective, such as zephiran chloride; alcohols, such as isopropyl and ethanol; various histologic fixatives, such as Bouin's fixative and Helly's fixative (see Humason, 1967); or a combination of physical (heat) and chemical agents that prolong the activity of the δ-endotoxin produced in the cell when the cell is applied to the environment of the target pest(s). Examples of physical means are short wavelength radiation such as gamma-radiation and X-radiation, freezing, UV irradiation, lyophilization, and the like.
The inventors contemplate that any formulation methods known to those of skill in the art may be employed using the proteins disclosed herein to prepare such bioinsecticide compositions. It may be desirable to formulate whole cell preparations, cell extracts, cell suspensions, cell homogenates, cell lysates, cell supernatants, cell filtrates, or cell pellets of a cell culture (preferably a bacterial cell culture such is a B. thuringiensis cell culture described in Table 3) that expresses one or more cry3Bb* DNA segments to produce the encoded Cry3Bb* protein(s) or peptide(s). The methods for preparing such formulations are known to those of skill in the art, and may include, e.g., desiccation, lyophilization, homogenization, extraction, filtration, centrifugation, sedimentation, or concentration of one or more cultures of bacterial cells, such as B. thuringiensis cells described in Table 3, which express the Cry3Bb* peptide(s) of interest.
In one preferred embodiment, the bioinsecticide composition comprises an oil flowable suspension comprising lysed or unlysed bacterial cells, spores, or crystals which contain one or more of the novel crystal proteins disclosed herein. Preferably the cells are B. thuringiensis cells, however, any such bacterial host cell expressing the novel nucleic acid segments disclosed herein and producing a crystal protein is contemplated to be useful, such as Bacillus spp., including B. megaterium, B. subtitis; B. cereus, Escherichia spp., including E. coli, and/or Pseudomonas spp., including P. cepacia, P. aeruginosa, and P. fluorescens. Alternatively, the oil flowable suspension may consist of a combination of one or more of the following compositions: lysed or unlysed bacterial cells, spores, crystals, and/or purified crystal proteins.
In a second preferred embodiment, the bioinsecticide composition comprises a water dispersible granule or powder. This granule or powder may comprise lysed or unlysed bacterial cells, spores, or crystals which contain one or more of the novel crystal proteins disclosed herein. Preferred sources for these compositions include bacterial cells such as B. thuringiensis cells, however, bacteria of the genera Bacillus, Escherichia, and Pseudomonas which have been transformed with a DNA segment disclosed herein and expressing the crystal protein are also contemplated to be useful. Alternatively, the granule or powder may consist of a combination of one or more of the following compositions: lysed or unlysed bacterial cells, spores, crystals, and/or purified crystal proteins.
In a third important embodiment, the bioinsecticide composition comprises a wettable powder, spray, emulsion, colloid, aqueous or organic solution, dust, pellet, or collodial concentrate. Such a composition may contain either unlysed or lysed bacterial cells, spores, crystals, or cell extracts as described above, which contain one or more of the novel crystal proteins disclosed herein. Preferred bacterial cells are B. thuringiensis cells, however, bacteria such as B. megaterium, B. subtilis, B. cereus, E. coli, or Pseudomonas spp. cells transformed with a DNA segment disclosed herein and expressing the crystal protein are also contemplated to be useful. Such dry forms of the insecticidal compositions may be formulated to dissolve immediately upon wetting, or alternatively, dissolve in a controlled-release, sustained-release, or other time-dependent manner. Alternatively, such a composition may consist of a combination of one or more of the following compositions: lysed or unlysed bacterial cells, spores, crystals, and/or purified crystal proteins.
In a fourth important embodiment, the bioinsecticide composition comprises an aqueous solution or suspension or cell culture of lysed or unlysed bacterial cells, spores, crystals, or a mixture of lysed or unlysed bacterial cells, spores, and/or crystals, such as those described above which contain one or more of the novel crystal proteins disclosed herein. Such aqueous solutions or suspensions may be provided as a concentrated stock solution which is diluted prior to application, or alternatively, as a diluted solution ready-to-apply.
For these methods involving application of bacterial cells, the cellular host containing the Crystal protein gene(s) may be grown in any convenient nutrient medium, where the DNA construct provides a selective advantage, providing for a selective medium so that substantially all or all of the cells retain the B. thurinoiensis gene. These cells may then be harvested in accordance with conventional ways. Alternatively, the cells can be treated prior to harvesting.
When the insecticidal compositions comprise B. thuringiensis cells, spores, and/or crystals containing the modified crystal protein(s) of interest, such compositions may be formulated in a variety of ways. They may be employed as wettable powders, granules or dusts, by mixing with various inert materials, such as inorganic minerals (phyllosilicates, carbonates, sulfates, phosphates, and the like) or botanical materials (powdered corncobs, rice hulls, walnut shells, and the like). The formulations may include spreader-sticker adjuvants, stabilizing agents, other pesticidal additives, or surfactants. Liquid formulations may be aqueous-based or non-aqueous and employed as foams, suspensions, emulsifiable concentrates, or the like. The ingredients may include rheological agents, surfactants, emulsifiers, dispersants, or polymers.
Alternatively, the novel Cry3Bb-derived mutated crystal proteins may be prepared by native or recombinant bacterial expression systems in vitro and isolated for subsequent field application. Such protein may be either in crude cell lysates, suspensions, colloids, etc., or alternatively may be purified, refined, buffered, and/or further processed, before formulating in an active biocidal formulation. Likewise, under certain circumstances, it may be desirable to isolate crystals and/or spores from bacterial cultures expressing the crystal protein and apply solutions, suspensions, or collodial preparations of such crystals and/or spores as the active bioinsecticidal composition.
Another important aspect of the invention is a method of controlling coleopteran insects which are susceptible to the novel compositions disclosed herein. Such a method generally comprises contacting the insect or insect population, colony, etc., with an insecticidally-effective amount of a Cry3Bb* crystal protein composition. The method may utilize Cry3Bb* crystal proteins such as those disclosed in SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34 SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, or SEQ ID NO:108, or biologically functional equivalents thereof.
Alternatively, the method may utilize one or more Cry3Bb* crystal proteins which are encoded by the nucleic acid sequences of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107, or by one or more nucleic acid sequences which hybridize to the sequences of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107, under conditions of moderate, or higher, stringency. The methods for identifying sequences which hybridize to those disclosed under conditions of moderate or higher stringency are well-known to those of skill in the art, and are discussed herein.
Regardless of the method of application, the amount of the active component(s) are applied at an insecticidally-effective amount, which will vary depending on such factors as, for example, the specific coleopteran insects to be controlled, the specific plant or crop to be treated, the environmental conditions, and the method, rate, and quantity of application of the insecticidally-active composition.
The insecticide compositions described may be made by formulating either the bacterial cell, crystal and/or spore suspension, or isolated protein component with the desired agriculturally-acceptable carrier. The compositions may be formulated prior to administration in an appropriate means such as lyophilized, freeze-dried, dessicated, or in an aqueous carrier, medium or suitable diluent, such as saline or other buffer. The formulated compositions may be in the form of a dust or granular material, or a suspension in oil (vegetable or mineral), or water or oil/water emulsions, or as a wettable powder, or in combination with any other carrier material suitable for agricultural application. Suitable agricultural carriers can be solid or liquid and are well known in the art. The term "agriculturally-acceptable carrier" covers all adjuvants, e.g., inert components, dispersants, surfactants, tackifiers, binders, etc. that are ordinarily used in insecticide formulation technology; these are well known to those skilled in insecticide formulation. The formulations may be mixed with one or more solid or liquid adjuvants and prepared by various means, e.g., by homogeneously mixing, blending and/or grinding the insecticidal composition with suitable adjuvants using conventional formulation techniques.
The insecticidal compositions of this invention are applied to the environment of the target coleopteran insect, typically onto the foliage of the plant or crop to be protected, by conventional methods, preferably by spraying. The strength and duration of insecticidal application will be set with regard to conditions specific to the particular pest(s), crop(s) to be treated and particular environmental conditions. The proportional ratio of active ingredient to carrier will naturally depend on the chemical nature, solubility, and stability of the insecticidal composition, as well as the particular formulation contemplated.
Other application techniques, e.g., dusting, sprinkling, soaking, soil injection, soil tilling, seed coating, seedling coating, spraying, aerating, misting, atomizing, and the like, are also feasible and may be required under certain circumstances such as e.g., insects that cause root or stalk infestation, or for application to delicate vegetation or ornamental plants. These application procedures are also well-known to those of skill in the art.
The insecticidal composition of the invention may be employed in the method of the invention singly or in combination with other compounds, including and not limited to other pesticides. The method of the invention may also be used in conjunction with other treatments such as surfactants, detergents, polymers or time-release formulations. The insecticidal compositions of the present invention may be formulated for either systemic or topical use.
The concentration of insecticidal composition which is used for environmental, systemic, or foliar application will vary widely depending upon the nature of the particular formulation, means of application, environmental conditions, and degree of biocidal activity. Typically, the bioinsecticidal composition will be present in the applied formulation at a concentration of at least about 1% by weight and may be up to and including about 99% by weight. Dry formulations of the compositions may be from about 1% to about 99% or more by weight of the composition, while liquid formulations may generally comprise from about 1% to about 99% or more of the active ingredient by weight. Formulations which comprise intact bacterial cells will generally contain from about 104 to about 1012 cells/mg.
The insecticidal formulation may be administered to a particular plant or target area in one or more applications as needed, with a typical field application rate per hectare ranging on the order of from about 1 g to about 1 kg, 2 kg, 5, kg, or more of active ingredient.
In addition to their use in directing the expression of crystal proteins or peptides of the present invention, the nucleic acid sequences contemplated herein also have a variety of other uses. For example, they also have utility as probes or primers in nucleic acid hybridization embodiments. As such, it is contemplated that nucleic acid segments that comprise a sequence region that consists of at least a 14 nucleotide long contiguous sequence that has the same sequence as, or is complementary to, a 14 nucleotide long contiguous DNA segment of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107 will find particular utility. Longer contiguous identical or complementary sequences, e.g, those of about 20, 30, 40, 50, 100, 200, 500, 1000, 2000, 5000, 10000 etc. (including all intermediate lengths and up to and including full-length sequences will also be of use in certain embodiments.
The ability of such nucleic acid probes to specifically hybridize to crystal protein-encoding sequences will enable them to be of use in detecting the presence of complementary sequences in a given sample. However, other uses are envisioned, including the use of the sequence information for the preparation of mutant species primers, or primers for use in preparing other genetic constructions.
Nucleic acid molecules having sequence regions consisting of contiguous nucleotide stretches of 10-14, 15-20, 30, 50, or even of 100-200 nucleotides or so, identical or complementary to DNA sequences of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5. SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13. SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, SEQ ID NO:101, or SEQ ID NO:107 are particularly contemplated as hybridization probes for use in, e.g., Southern and Northern blotting. Smaller fragments will generally find use in hybridization embodiments, wherein the length of the contiguous complementary region may be varied, such as between about 10-14 and about 100 or 200 nucleotides, but larger contiguous complementary stretches may be used, according to the length complementary sequences one wishes to detect.
The use of a hybridization probe of about 14 nucleotides in length allows the formation of a duplex molecule that is both stable and selective. Molecules having contiguous complementary sequences over stretches greater than 14 bases in length are generally preferred, though, in order to increase stability and selectivity of the hybrid, and thereby improve the quality and degree of specific hybrid molecules obtained. One will generally prefer to design nucleic acid molecules having gene-complementary stretches of 15 to 20 contiguous nucleotides, or even longer where desired.
Of course, fragments may also be obtained by other techniques such as, e.g., by mechanical shearing or by restriction enzyme digestion. Small nucleic acid segments or fragments may be readily prepared by, for example, directly synthesizing the fragment by chemical means, as is commonly practiced using an automated oligonucleotide synthesizer. Also, fragments may be obtained by application of nucleic acid reproduction technology, such as the PCR™ technology of U.S. Pat. Nos. 4,683,195 and 4,683,202 (each incorporated herein by reference), by introducing selected sequences into recombinant vectors for recombinant production, and by other recombinant DNA techniques generally known to those of skill in the art of molecular biology.
Accordingly, the nucleotide sequences of the invention may be used for their ability to selectively form duplex molecules with complementary stretches of DNA fragments. Depending on the application envisioned, one will desire to employ varying conditions of hybridization to achieve varying degrees of selectivity of probe towards target sequence. For applications requiring high selectivity, one will typically desire to employ relatively stringent conditions to form the hybrids., e.g., one will select relatively low salt and/or high temperature conditions, such as provided by about 0.02 M to about 0.15 M NaCl at temperatures of about 50° C. to about 70° C. Such selective conditions tolerate little, if any, mismatch between the probe and the template or target strand, and would be particularly suitable for isolating crystal protein-encoding DNA segments. Detection of DNA segments via hybridization is well-known to those of skill in the art, and the teachings of U.S. Pat. Nos. 4,965,188 and 5,176,995 (each incorporated herein by reference) are exemplary of the methods of hybridization analyses. Teachings such as those found in the texts of Maloy et al., 1994; Segal 1976; Prokop, 1991; and Kuby, 1994, are particularly relevant.
Of course, for some applications, for example, where one desires to prepare mutants employing a mutant primer strand hybridized to an underlying template or where one seeks to isolate crystal protein-encoding sequences from related species, functional equivalents, or the like, less stringent hybridization conditions will typically be needed in order to allow formation of the heteroduplex. In these circumstances, one may desire to employ conditions such as about 0.15 M to about 0.9 M salt, at temperatures ranging from about 20° C. to about 55° C. Cross-hybridizing species can thereby be readily identified as positively hybridizing signals with respect to control hybridizations. In any case, it is generally appreciated that conditions can be rendered more stringent by the addition of increasing amounts of formamide, which serves to destabilize the hybrid duplex in the same manner as increased temperature. Thus, hybridization conditions can be readily manipulated, and thus will generally be a method of choice depending on the desired results.
In certain embodiments, it will be advantageous to employ nucleic acid sequences of the present invention in combination with an appropriate means, such as a label, for determining hybridization. A wide variety of appropriate indicator means are known in the art, including fluorescent, radioactive, enzymatic or other ligands, such as avidin/biotin, which are capable of giving a detectable signal. In preferred embodiments, one will likely desire to employ a fluorescent label or an enzyme tag, such as urease, alkaline phosphatase or peroxidase, instead of radioactive or other environmental undesirable reagents. In the case of enzyme tags, colorimetric indicator substrates are known that can be employed to provide a means visible to the human eye or spectrophotometrically, to identify specific hybridization with complementary nucleic acid-containing samples.
In general, it is envisioned that the hybridization probes described herein will be useful both as reagents in solution hybridization as well as in embodiments employing a solid phase. In embodiments involving a solid phase, the test DNA (or RNA) is adsorbed or otherwise affixed to a selected matrix or surface. This fixed, single-stranded nucleic acid is then subjected to specific hybridization with selected probes under desired conditions. The selected conditions will depend on the particular circumstances based on the particular criteria required (depending, for example, on the G+C content, type of target nucleic acid, source of nucleic acid, size of hybridization probe, etc.). Following washing of the hybridized surface so as to remove nonspecifically bound probe molecules, specific hybridization is detected, or even quantitated, by means of the label.
The present invention provides novel polypeptides that define a whole or a portion of a B. thuringiensis cry3Bb.60, cry3Bb.11221, cry3Bb.11222, cry3Bb.11223, cry3Bb.11224, cry3Bb.11225, cry3Bb.11226, cry3Bb.11227, cry3Bb.11228, cry3Bb.11229, cry3Bb.11230, cry3Bb.11231, cry3Bb.11232, cry3Bb.11233, cry3Bb.11234, cry3Bb.11235, cry3Bb.11236, cry3Bb.11237, cry3Bb.11238, cry3Bb.11239, cry3Bb.11241, cry3Bb.11242, cry3Bb.11032, cry3Bb.11035, cry3Bb.11036, cry3Bb.11046, cry3Bb.11048, cry3Bb.11051, cry3Bb.11057, cry3Bb.11058, cry3Bb.11081, cry3Bb.11082, cry3Bb.11083, cry3Bb.11084, cry3Bb.11095 and cry3Bb.11098-encoded crystal protein.
The inventors have arbitrarily assigned the designations Cry3Bb.60, Cry3Bb.11221, Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11234, Cry3Bb.11235, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11032, Cry3Bb.11035, Cry3Bb.11036, Cry3Bb.11046, Cry3Bb.11048, Cry3Bb.11051, Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11095 and Cry3Bb.11098 to the novel proteins of the invention.
Likewise, the arbitrary designations of cry3Bb.60, cry3Bb.11221, cry3Bb.11222, cry3Bb.11223, cry3Bb.11224, cry3Bb.11225, cry3Bb.11226, cry3Bb.11227, cry3Bb.11228, cry3Bb.11229, cry3Bb.11230, cry3Bb.11231, cry3Bb.11232, cry3Bb.11233, cry3Bb.11234, cry3Bb.11235, cry3Bb.11236, cry3Bb.11237, cry3Bb.11238, cry3Bb.11239, cry3Bb.11241, cry3Bb.11242, cry3Bb.11032, cry3Bb.11035, cry3Bb.11036, cry3Bb.11046, cry3Bb.11048, cry3Bb.11051, cry3Bb.11057, cry3Bb.11058, cry3Bb.11081, cry3Bb.11082, cry3Bb.11083, cry3Bb.11084, cry3Bb.11095 and Cry3Bb.11098 have been assigned to the novel nucleic acid sequences which encode these polypeptides, respectively. While formal assignment of gene and protein designations based on the revised nomenclature of crystal protein endotoxins (Table 1) may be made by the committee on the nomenclature of B. thuringiensis, any re-designations of the compositions of the present invention are also contemplated to be fully within the scope of the present disclosure.
A bacterium, a yeast cell, or a plant cell or a plant transformed with an expression vector of the present invention is also contemplated. A transgenic bacterium, yeast cell, plant cell or plant derived from such a transformed or transgenic cell is also one aspect of the invention.
Such transformed host cells are often desirable for use in the production of endotoxins and for expression of the various DNA gene constrcuts disclosed herein. In some aspects of the invention, it is often desirable to modulate, regulate, or otherwise control the expression of the gene segments disclosed herein. Such methods are routine to those of skill in the molecular genetic arts. Typically, when increased or over-expression of a particular gene is desired, various manipulations may be employed for enhancing the expression of the messenger RNA, particularly by using an active promoter, as well as by employing sequences, which enhance the stability of the messenger RNA in the particular transformed host cell.
Typically, the initiation and translational termination region will involve stop codon(s), a terminator region, and optionally, a polyadenylation signal. In the direction of transcription, namely in the 5' to 3' direction of the coding or sense sequence, the construct will involve the transcriptional regulatory region, if any, and the promoter, where the regulatory region may be either 5' or 3' of the promoter, the ribosomal binding site, the initiation codon, the structural gene having an open reading frame in phase with the initiation codon, the stop codon(s), the polyadenylation signal sequence, if any, and the terminator region. This sequence as a double strand may be used by itself for transformation of a microorganism host, but will usually be included with a DNA sequence involving a marker, where the second DNA sequence may be joined to the δ-endotoxin expression construct during introduction of the DNA into the host.
By a marker is intended a structural gene which provides for selection of those hosts which have been modified or transformed. The marker will normally provide for selective advantage, for example, providing for biocide resistance, e.g., resistance to antibiotics or heavy metals; complementation, so as to provide prototropy to an auxotrophic host, or the like. Preferably, complementation is employed, so that the modified host may not only be selected, but may also be competitive in the field. One or more markers may be employed in the development of the constructs, as well as for modifying the host. The organisms may be further modified by providing for a competitive advantage against other wild-type microor- ganisms in the field. For example, genes expressing metal chelating agents, e.g., siderophores, may be introduced into the host along with the structural gene expressing the δ-endotoxin. In this manner, the enhanced expression of a siderophore may provide for a competitive advantage for the δ-endotoxin-producing host, so that it may effectively compete with the wild-type microorganisms and stably occupy a niche in the environment.
Where no functional replication system is present, the construct will also include a sequence of at least 50 basepairs (bp), preferably at least about 100 bp, and usually not more than about 1000 bp of a sequence homologous with a sequence in the host. In this way, the probability of legitimate recombination is enhanced, so that the gene will be integrated into the host and stably maintained by the host. Desirably, the δ-endotoxin gene will be in close proximity to the gene providing for complementation as well as the gene providing for the competitive advantage. Therefore, in the event that a δ-endotoxin gene is lost, the resulting organism will be likely to also lose the complementing gene and/or the gene providing for the competitive advantage, so that it will be unable to compete in the environment with the gene retaining the intact construct.
The crystal protein-encoding gene can be introduced between the transcriptional and translational initiation region and the transcriptional and translational termination region, so as to be under the regulatory control of the initiation region. This construct will be in- cluded in a plasmid, which will include at least one replication system, but may include more than one, where one replication system is employed for cloning during the development of the plasmid and the second replication system is necessary for functioning in the ultimate host. In addition, one or more markers may be present, which have been described previously. Where integration is desired, the plasmid will desirably include a sequence homologous with the host genome.
The transformants can be isolated in accordance with conventional ways, usually employing a selection technique, which allows for selection of the desired organism as against unmodified organisms or transferring organisms, when present. The transformants then can be tested for pesticidal activity.
Suitable host cells, where the pesticide-containing cells will be treated to prolong the activity of the δ-endotoxin in the cell when the then treated cell is applied to the environment of target pest(s), may include either prokaryotes or eukaryotes, normally being limited to those cells which do not produce substances toxic to higher organisms, such as mammals. However, organisms which produce substances toxic to higher organisms could be used, where the δ-endotoxin is unstable or the level of application sufficiently low as to avoid any possibility of toxicity to a mammalian host. As hosts, of particular interest will be the prokaryotes and the lower eukaryotes, such as fungi. Illustrative prokaryotes, both Gram-negative and -positive, include Enterobacteriaceae, such as Escherichia, Erwinia, Shigella, Salmonella, and Proteus; Bacillaceae; Rhizobiceae., such as Rhizobium; Spirillaceae, such as photobacterium, Zymomonas, Serratia, Aeromonas, Vibrio, Desulfovibdo, Spirillum; Lactobacillaceae; phylloplane organisms such as members of the Pseudomonadaceae (including Pseudomonas spp. and Acetobacter spp.); Azotobcacteraceae and Nitrobacteraceae; Flavobacterium spp.; members of the Bacillaceae such as Lactobacillus spp., Bifidobacterium, and Bacillus spp., and the like. Particularly preferred host cells include Pseudomonas aeruginosa, Pseudomonas fluorescens, Bacillus thuringiensis, Escherichia coli, Bacillus subtilis, and the like.
Among eukaryotes are fungi, such as Plycomycetes and Ascomycetes, which includes yeast, such as Schizosaccharomyces; and Basidiomycetes, Rhodotorula, Aureobasidium, Sporobolomyces, Saccharomyces spp., and Spotobolomyces spp.
Characteristics of particular interest in selecting a host cell for purposes of production include ease of introducing the δ-endotoxin gene into the host, availability of expression systems, efficiency of expression, stability of the pesticide in the host, and the presence of auxiliary genetic capabilities. Characteristics of interest for use as a pesticide microcapsule include protective qualities for the pesticide, such as thick cell walls, pigmentation, and intracellular packaging or formation of inclusion bodies; leaf affinity; lack of mammalian toxicity; attractiveness to pests for ingestion; ease of killing and fixing without damage to the δ-endotoxin; and the like. Other considerations include ease of formulation and handling, economics, storage stability, and the like.
The cell will usually be intact and be substantially in the proliferative form when treated, rather than in a spore form, although in some instances spores may be employed. Treatment of the recombinant microbial cell can be done as disclosed infra. The treated cells generally will have enhanced structural stability which will enhance resistance to environmental conditions.
Genes or other nucleic acid segments, as disclosed herein, can be inserted into host cells using a variety of techniques which are well known in the art. For example, a large number of cloning vectors comprising a replication system in E. coli and a marker that permits selection of the transformed cells are available for preparation for the insertion of foreign genes into higher organisms, including plants. The vectors comprise, for example, pBR322, pUC series, M13mp series, pACYC184, etc. Accordingly, the sequence coding for the δ-endotoxin can be inserted into the vector at a suitable restriction site. The resulting plasmid is used for transformation into E. coli. The E. coli cells are cultivated in a suitable nutrient medium, then harvested and lysed. The plasmid is recovered. Sequence analysis, restriction analysis, electrophoresis, and other biochemical-molecular biological methods are generally carried out as methods of analysis. After each manipulation, the DNA sequence used can be cleaved and joined to the next DNA sequence. Each plasmid sequence can be cloned in the same or other plasmids. Depending on the method of inserting desired genes into the plant, other DNA sequences may be necessary.
Methods for DNA transformation of plaint cells include Agrobacterium-mediated plant transformation, protoplast transformation, gene transfer into pollen, injection into reproductive organs, injection into immature embryos and particle bombardment. Each of these methods has distinct advantages and disadvantages. Thus, one particular method of introducing genes into a particular plant strain may not necessarily be the most effective for another plant strain, but it is well known which methods are useful for a particular plant strain.
Suitable methods are believed to include virtually any method by which DNA can be introduced into a cell, such as by Agrobacterium infection, direct delivery of DNA such as, for example, by PEG-mediated transformation of protoplasts (Omirulleh et al., 1993), by desiccation/inhibition-mediated DNA uptake, by electroporation, by agitation with silicon carbide fibers, by acceleration of DNA coated particles, etc. In certain embodiments, acceleration methods are preferred and include, for example, microprojectile bombardment and the like.
Technology for introduction of DNA into cells is well-known to those of skill in the art. Four general methods for delivering a gene into cells have been described: (1) chemical methods (Graham and van der Eb, 1973; Zatloukal et al., 1992); (2) physical methods such as microinjection (Capecchi, 1980), electroporation (Wong and Neumann, 1982; Fromm et al., 1985) and the gene gun (Johnston and Tang, 1994; Fynan et al., 1993); (3) viral vectors (Clapp, 1993; Lu et al., 1993; Eglitis and Anderson, 1988; Eglitis et al., 1988); and (4) receptor-mediated mechanisms (Curiel et al., 1991; 1992; Wagner et al., 1992).
A large number of techniques are available for inserting DNA into a plant host cell. Those techniques include transformation with T-DNA using Agrobacterium tumefaciens or Agrobactedum rhizogenes as transformation agent, fusion, injection, or electroporation as well as other possible methods. If agrobacteria are used for the transformation, the DNA to be inserted has to be cloned into special plasmid, namely either into an intermediate vector or into a binary vector. The intermediate vectors can be integrated into the Ti or Ri plasmid by homologous recombination owing to sequences that are homologous to sequences in the T-DNA. The Ti or Ri plasmid also comprises the vir region necessary for the transfer of the T-DNA.
Intermediate vectors cannot replicate themselves in agrobacteria. The intermediate vector can be transferred into Agrobacterium tumefaciens by means of a helper plasmid (conjugation). Binary vectors can replicate themselves both in E. coli and in agrobacteria. They comprise a selection marker gene and a linker or polylinker which are framed by the right and left T-DNA border regions. They can be transformed directly into agrobacteria (Holsters et al., 1978). The agrobacterium used as host cell is to comprise a plasmid carrying a vir region. The vir region is necessary for the transfer of the T-DNA into the plant cell. Additional t-DNA may be contained. The bacterium so transformed is used for the transformation of plant cells. Plant explants can advantageously be cultivated with Agrobacterium tumefaciens or Agrobacterium rhizogenes for the transfer of the DNA into the plant cell. Whole plants can then be regenerated from the infected plant material (for example, pieces of leaf, segments of stalk, roots, but also protoplasts or suspension-cultivated cells) in a suitable medium, which may contain antibiotics or biocides for selection. The plants so obtained can then be tested for the presence of the inserted DNA. No special demands are made of the plasmids in the case of injection and electroporation. It is possible to use ordinary plasmids, such as, for example, pUC derivatives. If, for example, the Ti or Ri plasmid is used for the transformation of the plant cell, then at least the right border, but often the right and the left border of the Ti or Ri plasmid T-DNA, has to be joined as the flanking region of the genes to be inserted. The use of T-DNA for the transformation of plant cells has been intensively researched and sufficiently described in Eur. Pat. Appl. No. EP 120 516; Hockema (1985); An et al., 1985, 1 Herrera-Estrella et al., (1983), Bevan et. al., (1983), and Klee et al, (1985).
A particularly useful Ti plasmid cassette vector for transformation of dicotyledonous plants consists of the enhanced CaMV35S promoter (EN35S) and the 3' end including polyadenylation signals from a soybean gene encoding the α'-subunit of β-conglycinin. Between these two elements is a multilinker containing multiple restriction sites for the insertion of genes of interest.
The vector preferably contains a segment of pBR322 which provides an origin of replication in E. coli and a region for homologous recombination with the disarmed T-DNA in Agrobacterium strain ACO; the oriV region from the broad host range plasmid RK1; the streptomycin/spectinomycin resistance gene from Tn7; and a chimeric NPTII gene, containing the CaMV35S promoter and the nopaline synthase (NOS) 3' end, which provides kanamycin resistance in transformed plant cells.
Optionally, the enhanced CaMV35S promoter may be replaced with the 1.5 kb mannopine synthase (MAS) promoter (Velten et al., 1984). After incorporation of a DNA construct into the vector, it is introduced into A. tumefaciens strain ACO which contains a disarmed Ti plasmid. Cointegrate Ti plasmid vectcors are selected and subsequentially may be used to transform a dicotyledonous plant.
A. tumefaciens ACO is a disarmed strain similar to pTiB6SE described by Fraley et al. (1985). For construction of ACO the starting Agrobacterium strain was the strain A208 which contains a nopaline-type Ti plasmid. The Ti plasmid was disarmed in a manner similar to that described by Fraley et al. (1985) so that essentially all of the native T-DNA was removed except for the left border and a few hundred base pairs of T-DNA inside the left border. The remainder of the T-DNA extending to a point just beyond the right border was replaced with a novel piece of DNA including (from left to right) a segment of pBR322, the oriV region from plasmid RK2, and the kanamycin resistance gene from Tn601. The pBR322 and oriV segments are similar to these segments and provide a region of homology for cointegrate formation.
Once the inserted DNA has been integrated in the genome, it is relatively stable there and, as a rule, does not come out again. It normally contains a selection marker that confers on the transformed plant cells resistance to a biocide or an antibiotic, such as kanamycin, G 418, bleomycin, hygromycin, or chloramphenicol, inter alia. The individually employed marker should accordingly permit the selection of transformed cells rather than cells that do not contain the inserted DNA.
The application of brief, high-voltage electric pulses to a variety of animal and plant cells leads to the formation of nanometer-sized pores in the plasma membrane. DNA is taken directly into the cell cytoplasm either through these pores or as a consequence of the redistribution of membrane components that accompanies closure of the pores. Electroporation can be extremely efficient and can be used both for transient expression of clones genes and for establishment of cell lines that carry integrated copies of the gene of interest. Electroporation, in contrast to calcium phosphate-mediated transfection and protoplast fusion, frequently gives rise to cell lines that carry one, or at most a few, integrated copies of the foreign DNA.
The introduction of DNA by means of electroporation, is well-known to those of skill in the art. In this method, certain cell wall-degrading enzymes, such as pectin-degrading enzymes, are employed to render the target recipient cells more susceptible to transformation by electroporation than untreated cells. Alternatively, recipient cells are made more susceptible to transformation, by mechanical Wounding. To effect transformation by electroporation one may employ either friable tissues such as a suspension culture of cells, or embryogenic callus, or alternatively, one may transform immature embryos or other organized tissues directly. One would partially degrade the cell walls of the chosen cells by exposing them to pectin-degrading enzymes (pectolyases) or mechanically wounding in a controlled manner. Such cells would then be recipient to DNA transfer by electroporation, which may be carried out at this stage, and transformed cells then identified by a suitable selection or screening protocol dependent on the nature of the newly incorporated DNA.
A further advantageous method for delivering transforming DNA segments to plant cells is microprojectile bombardment. In this method, particles may be coated with nucleic acids and delivered into cells by a propelling force. Exemplary particles include those comprised of tungsten, gold, platinum, and the like.
An advantage of microprojectile bombardment, in addition to it being an effective means of reproducibly stably transforming monocots, is that neither the isolation of protoplasts (Cristou et al., 1988) nor the susceptibility to Agrobacterium infection is required. An illustrative embodiment of a method for delivering DNA into maize cells by acceleration is a Biolistics Particle Delivery System, which can be used to propel particles coated with DNA or cells through a screen, such as a stainless steel or Nytex screen, onto a filter surface covered with corn cells cultured in suspension. The screen disperses the particles so that they are not delivered to the recipient cells in large aggregates. It is believed that a screen intervening between the projectile apparatus and the cells to be bombarded reduces the size of projectiles aggregate and may contribute to a higher frequency of transformation by reducing damage inflicted on the recipient cells by projectiles that are too large.
For the bombardment, cells in suspension are preferably concentrated on filters or solid culture medium. Alternatively, immature embryos or other target cells may be arranged on solid culture medium. The cells to be bombarded are positioned at an appropriate distance below the macroprojectile stopping plate. If desired, one or more screens are also positioned between the acceleration device and the cells to be bombarded. Through the use of techniques set forth herein one may obtain up to 1000 or more foci of cells transiently expressing a marker gene. The number of cells in a focus which express the exogenous gene product 48 hours post-bombardment often range from 1 to 10 and average 1 to 3.
In bombardment transformation, one may optimize the prebombardment culturing conditions and the bombardment parameters to yield the maximum numbers of stable transformants. Both the physical and biological parameters for bombardment are important in this technology. Physical factors are those that involve manipulating the DNA/microprojectile precipitate or those that affect the flight and velocity of either the macro- or microprojectiles. Biological factors include all steps involved in manipulation of cells before and immediately after bombardment, the osmotic adjustment of target cells to help alleviate the trauma associated with bombardment, and also the nature of the transforming DNA, such as linearized DNA or intact supercoiled plasmids. It is believed that pre-bombardment manipulations are especially important for successful transformation of immature embryos.
Accordingly, it is contemplated that one may wish to adjust various of the bombardment parameters in small scale studies to fully optimize the conditions. One may particularly wish to adjust physical parameters such as gap distance, flight distance, tissue distance, and helium pressure. One may also minimize the trauma reduction factors (TRFs) by modifying conditions which influence the physiological state of the recipient cells and which may therefore influence transformation and integration efficiencies. For example, the osmotic state, tissue hydration and the subculture stage or cell cycle of the recipient cells may be adjusted for optimum transformation. The execution of other routine adjustments will be known to those of skill in the art in light of the present disclosure.
Agrobacterium-mediated transfer is a widely applicable system for introducing genes into plant cells because the DNA can be introduced into whole plant tissues, thereby bypassing the need for regeneration of an intact plant from a protoplast. The use of Agrobacterium-mediated plant integrating vectors to introduce DNA into plant cells is well known in the art. See, for example, the methods described (Fraley et al., 1985; Rogers et al, 1987). Further, the integration of the Ti-DNA is a relatively precise process resulting in few rearrangements. The region of DNA to be transferred is defined by the border sequences, and intervening DNA is usually inserted into the plant genome as described (Spielmann et al., 1986; Jorgensen et al., 1987).
Modem Agrobacterium transformation vectors are capable of replication in E. coli as well as Agrobacterium, allowing for convenient manipulations as described (Klee et al., 1985). Moreover, recent technological advances in vectors for Agrobacterium-mediated gene transfer have improved the arrangement of genes and restriction sites in the vectors to facilitate construction of vectors capable of expressing various polypeptide coding genes. The vectors described (Rogers et al., 1987), have convenient multi-linker regions flanked by a promoter and a polyadenylation site for direct expression of inserted polypeptide coding genes and are suitable for present purposes. In addition, Agrobacterium containing both armed and disarmed Ti genes can be used for the transformations. In those plant strains where Agrobacterium-mediated transformation is efficient, it is the method of choice because of the facile and defined nature of the gene transfer.
Agrobacterium-mediated transformation of leaf disks and other tissues such as cotyledons and hypocotyls appears to be limited to plants that Agrobacterium naturally infects. Agrobacterium-mediated transformation is most efficient in dicotyledonous plants. Few monocots appear to be natural hosts for Agrobacterium, although transgenic plants have been produced in asparagus using Agrobacterium vectors as described (Bytebier et al., 1987). Therefore, commercially important cereal grains such as rice, corn, and wheat must usually be transformed using alternative methods. However, as mentioned above, the transformation of asparagus using Agrobacterium can also be achieved (see, for example, Bytebier et al., 1987).
A transgenic plant formed using Agrobacterium transformation methods typically contains a single gene on one chromosome. Such transgenic plants can be referred to as being heterozygous for the added gene. However, inasmuch as use of the word "heterozygous" usually implies the presence of a complementary gene at the same locus of the second chromosome of a pair of chromosomes, and there is no such gene in a plant containing one added gene as here, it is believed that a more accurate name for such a plant is an independent segregant, because the added, exogenous gene segregates independently during mitosis and meiosis.
More preferred is a transgenic plant that is homozygous for the added structural gene; i.e., a transgenic plant that contains two added genes, one gene at the same locus on each chromosome of a chromosome pair. A homozygous transgenic plant can be obtained by sexually mating (selfing) an independent segregant transgenic plant that contains a single added gene, germinating some of the seed produced and analyzing the resulting plants produced for enhanced carboxylase activity relative to a control (native, non-transgenic) or an independent segregant transgenic plant.
It is to be understood that two different transgenic plants can also be mated to produce offspring that contain two independently segregating added, exogenous genes. Selfing of appropriate progeny can produce plants that are homozygous for both added, exogenous genes that encode a polypeptide of interest. Back-crossing to a parental plant and out-crossing with a non-transgenic plant are also contemplated.
Transformation of plant protoplasts can be achieved using methods based on calcium phosphate precipitation, polyethylene glycol treatment, electroporation, and combinations of these treatments (see, e.g., Potrykus et al., 1985; Lorz et al., 1985; Fromm et al., 1985; Uchimiya et al., 1986; Callis et al., 1987; Marcotte et al., 1988).
Application of these systems to different plant strains depends upon the ability to regenerate that particular plant strain from protoplasts. Illustrative methods for the regeneration of cereals from protoplasts are described (Fujimura et al., 1985; Toriyama et al., 1986; Yamada et al., 1986; Abdullah et al, 1986).
To transform plant strains that cannot be successfully regenerated from protoplasts, other ways to introduce DNA into intact cells or tissues can be utilized. For example, regeneration of cereals from immature embryos or explants can be effected as described (Vasil, 1988). In addition, "particle gun" or high-velocity microprojectile technology can be utilized (Vasil, 1992).
Using that latter technology, DNA is carried through the cell wall and into the cytoplasm on the surface of small metal particles as described (Klein et al., 1987; Klein et al, 1988; McCabe et al., 1988). The metal particles penetrate through several layers of cells and thus allow the transformation of cells within tissue explants.
Although great progress has been made in recent years with respect to preparation of transgenic plants which express bacterial proteins such as B. thuringiensis crystal proteins, the results of expressing native bacterial genes in plants are often disappointing. Unlike microbial genetics, little was known by early plant geneticists about the factors which affected heterologous expression of foreign genes in plants. In recent years, however, several potential factors have been implicated as responsible in varying degrees for the level of protein expression from a particular coding sequence. For example, scientists now know that maintaining a significant level of a particular mRNA in the cell is indeed a critical factor. Unfortunately, the causes for low steady state levels of mRNA encoding foreign proteins are many. First, full length RNA synthesis may not occur at a high frequency. This could, for example, be caused by the premature termination of RNA during transcription or due to unexpected mRNA processing during transcription. Second, full length RNA may be produced in the plant cell, but then processed (splicing, polyA addition) in the nucleus in a fashion that creates a nonfunctional mRNA. If the RNA is not properly synthesized, terminated and polyadenylated, it cannot move to the cytoplasm for translation. Similarly, in the cytoplasm, if mRNAs have reduced half lives (which are determined by their primary or secondary sequence) inisufficient protein product will be produced. In addition, there is an effect, whose magnitude is uncertain, of translational efficiency on mRNA half-life. In addition, every RNA molecule folds into a particular structure, or perhaps family of structures, which is determined by its sequence. The particular structure of any RNA might lead to greater or lesser stability in the cytoplasm. Structure per se is probably also a determinant of mRNA processing in the nucleus. Unfortunately, it is impossible to predict, and nearly impossible to determine, the structure of any RNA (except for tRNA) in vitro or in vivo. However, it is likely that dramatically changing the sequence of an RNA will have a large effect on its folded structure It is likely that structure per se or particular structural features also have a role in determining RNA stability.
To overcome these limitations in foreign gene expression, researchers have identified particular sequences and signals in RNAs that have the potential for having a specific effect on RNA stability. In certain embodiments of the invention, therefore, there is a desire to optimize expression of the disclosed nucleic acid segments in planta. One particular method of doing so, is by alteration of the bacterial gene to remove sequences or motifs which decrease expression in a transformed plant cell. The process of engineering a coding sequence for optimal expression in planta is often referred to as "plantizing" a DNA sequence.
Particularly problematic sequences are those which are A+T rich. Unfortunately, since B. thuringiensis has an A+T rich genome, native crystal protein gene sequences must often be modified for optimal expression in a plant. The sequence motif ATTTA (or AUUUA as it appears in RNA) has been implicated as a destabilizing sequence in mammalian cell mRNA (Shaw and Kamen, 1986). Many short lived mRNAs have A+T rich 3' untranslated regions, and these regions often have the ATTTA sequence, sometimes present in multiple copies or as multimers (e.g., ATTTATTTA . . . ). Shaw and Kamen showed that the transfer of the 3' end of an unstable mRNA to a stable RNA (globin or VAl) decreased the stable RNA's half life dramatically. They further showed that a pentamer of ATTTA had a profound destabilizing effect on a stable message, and that this signal could exert its effect whether it was located at the 3' end or within the coding sequence. However, the number of ATTTA sequences and/or the sequence context in which they occur also appear to be important in determining whether they function as destabilizing sequences. Shaw and Kamen showed that a trimer of ATTTA had much less effect than a pentamer on mRNA stability and a dimer or a monomer had no effect on stability (Shaw and Kamen, 1987). Note that multimers of ATTTA such as a pentamer automatically create an A+T rich region. This was shown to be a cytoplasmic effect, not nuclear. In other unstable mRNAs, the ATTTA sequence may be present in only a single copy, but it is often contained in an A+T rich region. From the animal cell data collected to date, it appears that ATTTA at least in some contexts is important in stability but it is not yet possible to predict which occurrences of ATTTA are destabiling elements or whether any of these effects are likely to be seen in plants.
Some studies on mRNA degradation in animal cells also indicate that RNA degradation may begin in some cases with nucleolytic attack in A+T rich regions. It is not clear if these cleavages occur at ATTTA sequences. There are also examples of mRNAs that have differential stability depending on the cell type in which they are expressed or on the stage within the cell cycle at which they are expressed. For example, histone mRNAs are stable during DNA synthesis but unstable if DNA synthesis is disrupted. The 3' end of some histone mRNAs seems to be responsible for this effect (Pandey and Marzluff, 1987). It does not appear to be mediated by ATTTA, nor is it clear what controls the differential stability of this mRNA. Another example is the differential stability of IgG mRNA in B lymphocytes during B cell maturation (Genovese and Milcarek, 1988). A final example is the instability of a mutant β-thallesemic globin mRNA. In bone marrow cells, where this gene is normally expressed, the mutant mRNA is unstable, while the wild-type mRNA is stable. When the mutant gene is expressed in HeLa or L cells in vitro, the mutant mRNA shows no instability (Lim et al., 1988). These examples all provide evidence that mRNA stability can be mediated by cell type or cell cycle specific factors. Furthermore this type of instability is not yet associated with specific sequences. Given these uncertainties, it is not possible to predict which RNAs are likely to be unstable in a given cell. In addition, even the ATTTA motif may act differentially depending on the nature of the cell in which the RNA is present. Shaw and Kamen (1987) have reported that activation of protein kinase C can block degradation mediated by ATTTA.
The addition of a polyadenylate string to the 3' end is common to most eukaryotic mRNAs, both plant and animal. The currently accepted view of polyA addition is that the nascent transcript extends beyond the mature 3' terminus. Contained within this transcript are signals for polyadenylation and proper 3' end formation. This processing at the 3' end involves cleavage of the mRNA and addition of polyA to the mature 3' end. By searching for consensus sequences near the polyA tract in both plant and animal mRNAs, it has been possible to identify consensus sequences that apparently are involved in polyA addition and 3' end cleavage. The same consensus sequences seem to be important to both of these processes. These signals are typically a variation on the sequence AATAAA. In animal cells, some variants of this sequence that are functional have been identified; in plant cells there seems to be an extended range of functional sequences (Wickens and Stephenson, 1984; Dean et al., 1986). Because all of these consensus sequences are variations on AATAAA, they all are A+T rich sequences. This sequence is typically found 15 to 20 bp before the polyA tract in a mature mRNA. Studies in animal cells indicate that this sequence is involved in both polyA addition and 3' maturation. Site directed mutations in this sequence can disrupt these functions (Conway and Wickens, 1988; Wickens et al., 1987). However, it has also been observed that sequences up to 50 to 100 bp 3' to the putative polyA signal are also required; i.e., a gene that has a normal AATAAA but has been replaced or disrupted downstream does not get properly polyadenylated (Gil and Proudfoot, 1984; Sadofsky and Alwine, 1984; McDevitt et al., 1984). That is, the polyA signal itself is not sufficient for complete and proper processing. It is not yet known what specific downstream sequences are required in addition to the polyA signal, or if there is a specific sequence that has this function. Therefore, sequence analysis can only identify potential polyA signals.
In naturally occurring mRNAs that are normally polyadenylated, it has been observed that disruption of this process, either by altering the polyA signal or other sequences in the mRNA, profound effects can be obtained in the level of functional mRNA. This has been observed in several naturally occurring mRNAs, with results that are gene-specific so far.
It has been shown that in natural mRNAs proper polyadenylation is important in mRNA accumulation, and that disruption of this process can effect mRNA levels significantly. However, insufficient knowledge exists to predict the effect of changes in a normal gene. In a heterologous gene, it is even harder to predict the consequences. However, it is possible that the putative sites identified are dysfunctional. That is, these sites may not act as proper polyA sites, but instead function as aberrant sites that give rise to unstable mRNAs.
In animal cell systems, AATAAA is by far the most common signal identified in mRNAs upstream of the polyA, but at least four variants have also been found (Wickens and Stephenson, 1984). In plants, not nearly so much analysis has been done, but it is clear that multiple sequences similar to AATAAA can be used. The plant sites in Table 5 called major or minor refer only to the study of Dean et al. (1986) which analyzed only three types of plant gene. The designation of polyadenylation sites as major or minor refers only to the frequency of their occurrence as functional sites in naturally occurring genes that have been analyzed. In the case of plants this is a very limited database. It is hard to predict with any certainty that a site designated major or minor is more or less likely to function partially or completely when found in a heterologous gene such as those encoding the crystal proteins of the present invention.
TABLE 5 ______________________________________ POLYADENYLATION SITES IN PLANT GENES ______________________________________ PA AATAAA Major consensus site P1A AATAAT Major plant site P2A AACCAA Minor plant site P3A ATATAA " P4A AATCAA " P5A ATACTA " P6A ATAAAA " P7A ATGAAA " P8A AAGCAT " P9A ATTAAT " P10A ATACAT " P11A AAAATA " P12A ATTAAA Minor animal site P13A AATTAA " P14A AATACA " P15A CATAAA " ______________________________________
The present invention provides a method for preparing synthetic plant genes which genes express their protein product at levels significantly higher than the wild-type genes which were commonly employed in plant transformation heretofore. In another aspect, the present invention also provides novel synthetic plant genes which encode non-plant proteins.
As described above, the expression of native B. thuringiensis genes in plants is often problematic. The nature of the coding sequences of B. thuringiensis genes distinguishes them from plant genes as well as many other heterologous genes expressed in plants. In particular, B. thuringiensis genes are very rich (˜62%) in adenine (A) and thymine (T) while plant genes and most other bacterial genes which have been expressed in plants are on the order of 45-55% A+T.
Due to the degeneracy of the genetic code and the limited number of codon choices for any amino acid, most of the "excess" A+T of the structural coding sequences of some Bacillus species are found in the third position of the codons. That is, genes of some Bacillus species have A or T as the third nucleotide in many codons. Thus A+T content in part can determine codon usage bias. In addition, it is clear that genes evolve for maximum function in the organism in which they evolve. This means that particular nucleotide sequences found in a gene from one organism, where they may play no role except to code for a particular stretch of amino acids, have the potential to be recognized as gene control elements in another organism (such as transcriptional promoters or terminators, polyA addition sites, intron splice sites, or specific mRNA degradation signals). It is perhaps surprising that such misread signals are not a more common feature of heterologous gene expression, but this can be explained in part by the relatively homogeneous A+T content (˜50%) of many organisms. This A+T content plus the nature of the genetic code put clear constraints on the likelihood of occurrence of any particular oligonucleotide sequence. Thus, a gene from E. coli with a 50% A+T content is much less likely to contain any particular A+T rich segment than a gene from B. thuringiensis.
Typically, to obtain high-level expression of the S-endotoxin genes in plants, existing structural coding sequence ("structural gene") which codes for the S-endotoxin are modified by removal of ATTTA sequences and putative polyadenylation signals by site directed mutagenesis of the DNA comprising the structural gene. It is most preferred that substantially all the polyadenylation signals and ATTTA sequences are removed although enhanced expression levels are observed with only partial removal of either of the above identified sequences. Alternately if a synthetic gene is prepared which codes for the expression of the subject protein, codons are selected to avoid the ATTTA sequence and putative polyadenylation signals. For purposes of the present invention putative polyadenylation signals include, but are not necessarily limited to, AATAAA, AATAAT, AACCAA, ATATAA, AATCAA, ATACTA, ATAAAA, ATGAAA, AAGCAT, ATTAAT, ATACAT, AAAATA, ATTAAA, AATTAA, AATACA and CATAAA. In replacing the ATTTA sequences and polyadenylation signals, codons are preferably utilized which avoid the codons which are rarely found in plant genomes.
The selected DNA sequence is scanned to identify regions with greater than four consecutive adenine (A) or thymine (T) nucleotides. The A+T regions are scanned for potential plant polyadenylation signals. Although the absence of five or more consecutive A or T nucleotides eliminates most plant polyadenylation signals, if there are more than one of the minor polyadenylation signals identified within ten, nucleotides of each other, then the nucleotide sequence of this region is preferably altered to remove these signals while maintaining the original encoded amino acid sequence.
The second step is to consider the about 15 to about 30 or so nucleotide residues surrounding the A+T rich region identified in step one. If the A+T content of the surrounding region is less than 80%, the region should be examined for polyadenylation signals. Alteration of the region based on polyadenylation signals is dependent upon (1) the number of polyadenylation signals present and (2) presence of a major plant polyadenylation signal.
The extended region is examined for the presence of plant polyadenylation signals. The polyadenylation signals are removed by site-directed mutagenesis of the DNA sequence. The extended region is also examined for multiple copies of the ATTTA sequence which are also removed by mutagenesis.
It is also preferred that regions comprising many consecutive A+T bases or G+C bases are disrupted since these regions are predicted to have a higher likelihood to form hairpin structure due to self-complementarity. Therefore, insertion of heterogeneous base pairs would reduce the likelihood of self-complementary secondary structure formation which are known to inhibit transcription and/or translation in some organisms. In most cases, the adverse effects may be minimized by using sequences which do not contain more than five consecutive A+T or G+C.
When oligonucleotides are used in the mutagenesis, it is desirable to maintain the proper amino acid sequence and reading frame, without introducing common restriction sites such as BglII, HindIII, SacI, KpnI, EcoRI, NcoI, PstI and SalI into the modified gene. These restriction sites are found in poly-linker insertion sites of many cloning vectors. Of course, the introduction of new polyadenylation signals, ATTTA sequences or consecutive stretches of more than five A+T or G+C, should also be avoided. The preferred size for the oligonucleotides is about 40 to about 50 bases, but fragments ranging from about 18 to about 100 bases have been utilized. In most cases, a minimum of about 5 to about 8 base pairs of homology to the template DNA on both ends of the synthesized fragment are maintained to insure proper hybridization of the primer to the template. The oligonucleotides should avoid sequences longer than five base pairs A+T or G+C. Codons used in the replacement of wildtype codons should preferably avoid the TA or CG, doublet wherever possible. Codons are selected from a plant preferred codon table (such is Table 6 below) so as to avoid codons which are rarely found in plant genomes, and efforts should be made to select codons to preferably adjust the G+C content to about 50%.
TABLE 6
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PREFERRED CODON USAGE IN PLANTS
Percent Usage
Amino Acid Codon in Plants
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ARG CGA 7
CGC 11
CGG 5
CGU 25
AGA 29
AGG 23
LEU CUA 8
CUC 20
CUG 10
CUU 28
UUA 5
UUG 30
SER UCA 14
UCC 26
UCG 3
UCU 21
AGC 21
AGU 15
THR ACA 21
ACC 41
ACG 7
ACU 31
PRO CCA 45
CCC 19
CCG 9
CCU 26
ALA GCA 23
GCC 32
GCG 3
GCU 41
GLY GGA 32
GGC 20
GGG 11
GGU 37
ILE AUA 12
AUC 45
AUU 43
VAL GUA 9
GUC 20
GUG 28
GUU 43
LYS AAA 36
AAG 64
ASN AAC 72
AAU 28
GLN CAA 64
CAG 36
HIS CAC 65
CAU 35
GLU GAA 48
GAG 52
ASP GAC 48
GAU 52
TYR UAC 68
UAU 32
CYS UGC 78
UGU 22
PHE UUC 56
UUU 44
MET AUG 100
TRP UGG 100
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Regions with many consecutive A+T bases or G+C bases are predicted to have a higher likelihood to form hairpin structures due to self-complementarity. Disruption of these regions by the insertion of heterogeneous base pairs is preferred and should reduce the likelihood of the formation of self-complementary secondary structures such as hairpins which are known in some organisms to inhibit transcription (transcriptional terminators) and translation (attenuators).
Alternatively, a completely synthetic gene for a given amino acid sequence can be prepared, with regions of five or more consecutive A+T or G+C nucleotides being avoided. Codons are selected avoiding the TA and CG doublets in codons whenever possible. Codon usage can be normalized against a plant preferred codon usage table (such as Table 6) and the G+C content preferably adjusted to about 50%. The resulting sequence should be examined to ensure that there are minimal putative plant polyadenylation signals and ATTTA sequences. Restriction sites found in commonly used cloning vectors are also preferably avoided. However, placement of several unique restriction sites throughout the gene is useful for analysis of gene expression or construction of gene variants.
The expression of a plant gene which exists in double-stranded DNA form involves transcription of messenger RNA (mRNA) from one strand of the DNA by RNA polymerase enzyme, and the subsequent processing of the mRNA primary transcript inside the nucleus. This processing involves a 3' non-translated region which adds polyadenylate nucleotides to the 3' end of the RNA. Transcription of DNA into mRNA is regulated by a region of DNA usually referred to as the "promoter." The promoter region contains a sequence of bases that signals RNA polymerase to associate with the DNA and to initiate the transcription of mRNA using one of the DNA strands as a template to make a corresponding strand of RNA.
A number of promoters which are active in plant cells have been described in the literature. These include the nopaline synthase (NOS) and octopine synthase (OCS) promoters (which are carried on tumor-inducing plasmids of Agrobacterium tumefaciens), the Cauliflower Mosaic Virus (CaMV) 19S and 35S promoters, the light-inducible promoter from the small subunit of ribulose bis-phosphate carboxylase (ssRUBISCO, a very abundant plant polypeptide) and the mannopine synthase (MAS) promoter (Velten et al, 1984 and Velten and Schell, 1985). All of these promoters have been used to create various types of DNA constructs which have been expressed in plants (see e.g., Int. Pat. Appl. Publ. No. WO 84/02913).
Promoters which are known or are found to cause transcription of RNA in plant cells can be used in the present invention. Such promoters may be obtained from plants or plant viruses and include, but are not limited to, the CaMV35S promoter and promoters isolated from plant genes such as ssRUBISCO genes. As described below, it is preferred that the particular promoter selected should be capable of causing sufficient expression to result in the production of an effective amount of protein.
The promoters used in the DNA constructs (i.e. chimeric plant genes) of the present invention may be modified, if desired, to affect their control characteristics. For example, the CaMV35S promoter may be ligated to the portion of the ssRUBISCO gene that represses the expression of ssRUBISCO in the absence of light, to create a promoter which is active in leaves but not in roots. The resulting chimeric promoter may be used as described herein. For purposes of this description, the phrase "CaMV35S" promoter thus includes variations of CaMV35S promoter, e.g, promoters derived by means of ligation with operator regions, random or controlled mutagenesis, etc. Furthermore, the promoters may be altered to contain multiple "enhancer sequences" to assist in elevating gene expression.
The RNA produced by a DNA construct of the present invention also contains a 5' non-translated leader sequence. This sequence can be derived from the promoter selected to express the gene, and can be specifically modified so as to increase translation of the mRNA. The 5' non-translated regions can also be obtained from viral RNA's, from suitable eukaryotic genes, or from a synthetic gene sequence. The present invention is not limited to constructs, as presented in the following examples. Rather, the non-translated leader sequence can be part of the 5' end of the non-translated region of the coding sequence for the virus coat protein, or part of the promoter sequence, or can tie derived from an unrelated promoter or coding sequence. In any case, it is preferred that the sequence flanking the initiation site conform to the translational consensus sequence rules for enhanced translation initiation reported by Kozak (1984).
The cry DNA constructs of the present invention may also contain one or more modified or fully-synthetic structural coding sequences which have been changed to enhance the performance of the cry gene in plants. The structural genes of the present invention may optionally encode a fusion protein comprising an amino-terminal chloroplast transit peptide or secretory signal sequence.
The DNA construct also contains a 3' non-translated region. The 3' nontranslated region contains a polyadenylation signal which functions in plants to cause the addition of polyadenylate nucleotides to the 3' end of the viral RNA. Examples of suitable 3' regions are (1) the 3' transcribed, non-translated regions containing the polyadenylation signal of Agrobacterium tumor-inducing (Ti) plasmid genes, such as the nopaline synthase (NOS) gene, and (2) plant genes like the soybean storage protein (7S) genes and the small subunit of the RuBP carboxylase (E9) gene.
By transforming a suitable host cell, such as a plant cell, with a recombinant cry* gene-containing segment, the expression of the encoded crystal protein (i.e., a bacterial crystal protein or polypeptide having insecticidal activity against coleopterans) can result in the formation of insect-resistant plants.
By way of example, one may utilize an expression vector containing a coding region for a B. thuringiensis crystal protein and an appropriate selectable marker to transform a suspension of embryonic plant cells, such as wheat or corn cells using a method such as particle bombardment (Maddock et al., 1991; Vasil et al., 1992) to deliver the DNA coated on microprojectiles into the recipient cells. Transgenic plants are then regenerated from transformed embryonic calli that express the insecticidal proteins.
The formation of transgenic plants may also be accomplished using other methods of cell transformation which are known in the art such as Agrobacterium-mediated DNA transfer (Fraley et al., 1983). Alternatively, DNA. can be introduced into plants by direct DNA transfer into pollen (Zhou et al., 1983; Hess, 1987; Luo et al., 1988), by injection of the DNA into reproductive organs of a plant (Pena et al., 1987), or by direct injection of DNA into the cells of immature embryos followed by the rehydration of desiccated embryos (Neuhaus et al., 1987; Benbrook et al., 1986).
The regeneration, development, and cultivation of plants from single plant protoplast transformants or from various transformed explants is well known in the art (Weissbach and Weissbach, 1988). This regeneration and growth process typically includes the steps of selection of transformed cells, culturing those individualized cells through the usual stages of embryonic development through the rooted plantlet stage. Transgenic embryos and seeds are similarly regenerated. The resulting transgenic rooted shoots are thereafter planted in an appropriate plant growth medium such as soil.
The development or regeneration of plants containing the foreign, exogenous gene that encodes a polypeptide of interest introduced by Agrobacterium from leaf explants can be achieved by methods well known in the art such as described (Horsch et al., 1985). In this procedure, transformants are cultured in the presence of a selection agent and in a medium that induces the regeneration of shoots in the plant strain being transformed as described (Fraley et al., 1983 ).
This procedure typically produces shoots within two to four months and those shoots are then transferred to an appropriate root-inducing medium containing the selective agent and an antibiotic to prevent bacterial growth. Shoots that rooted in the presence of the selective agent to form plantlets are then transplanted to soil or other media to allow the production of roots. These procedures vary depending upon the particular plant strain employed, such variations being well known in the art.
Preferably, the regenerated plants are self-pollinated to provide homozygous transgenic plants, as discussed before. Otherwise, pollen obtained from the regenerated plants is crossed to seed-grown plants of agronomically important, preferably inbred lines. Conversely, pollen from plants of those important lines is used to pollinate regenerated plants. A transgenic plant of the present invention containing a desired polypeptide is cultivated using methods well known to one skilled in the art.
Such plants can form germ cells and transmit the transformed trait(s) to progeny plants. Likewise, transgenic plants can be grown in the normal manner and crossed with plants that have the same transformed hereditary factors or other hereditary factors. The resulting hybrid individuals have the corresponding phenotypic properties. A transgenic plant of this invention thus has an increased amount of a coding region (e.g., a mutated cry gene) that encodes the mutated Cry polypeptide of interest. A preferred transgenic plant is an independent segregant and can transmit that gene and its activity to its progeny. A more preferred transgenic plant is homozygous for that gene, and transmits that gene to all of its offspring on sexual mating.
Seed from a transgenic plant may be grown in the field or greenhouse, and resulting sexually mature transgenic plants are self-pollinated to generate true breeding plants. The progeny from these plants become true breeding lines that are evaluated for, by way of example, increased insecticidal capacity against coleopteran insects, preferably in the field, under a range of environmental conditions. The inventors contemplate that the present invention will find particular utility in the creation of transgenic plants of commercial interest including various grasses, grains, fibers, tubers, legumes, ornamental plants, cacti, succulents, fruits, berries, and vegetables, as well as a number of nut- and fruit-bearing trees and plants.
Crystal protein mutants containing substitutions in one or more domains may be constructed via a number of techniques. For instance, sequences of highly related genes can be readily shuffled using the PCR™-based technique described by Stemmer (1994). Alternatively, if suitable restriction sites are available, the mutations of one cry gene may be combined with the mutations of a second cry gene by routine subcloning methodologies. If a suitable restriction site is not available, one may be generated by oligonucleotide directed mutagenesis using any number of procedures known to those skilled in the art. Alternatively, splice-overlap extension PCR™ (Horton et al., 1989) may be used to combine mutations in different regions of a crystal protein. In this procedure, overlapping DNA fragments generated by the PCR™ and containing different mutations within their unique sequences may be annealed and used as a template for amplification u:sing flanking primers to generate a hybrid gene sequence. Finally, cry* mutants may be combined by simply using one cry mutant as a template for oligonucleotide-directed mutagenesis using any number of protocols such as those described herein.
The genes and δ-endotoxins according to the subject invention include not only the full length sequences disclosed herein but also fragments of these sequences, or fusion proteins, which retain the characteristic insecticidal activity of the sequences specifically exemplified herein.
It should be apparent to a person skill in this art that insecticidal δ-endotoxins can be identified and obtained through several means. The specific genes, or portions thereof, may be obtained from a culture depository, or constructed synthetically, for example, by use of a gene machine. Variations of these genes may be readily constructed using standard techniques for making point mutations. Also, fragments of these genes can be made using commercially available exonucleases or endonucleases according to standard procedures. For example, enzymes such as Bal31 or site-directed mutagenesis can be used to systematically cut off nucleotides from the ends of these genes. Also, genes which code for active fragments may be obtained using a variety of other restriction enzymes. Proteases may be used to directly obtain active fragments of these δ-endotoxins.
Equivalent δ-endotoxins and/or genes encoding these equivalent δ-endotoxins can also be isolated from Bacillus strains and/or DNA libraries using the teachings provided herein. For example, antibodies to the δ-endotoxins disclosed and claimed herein can be used to identify and isolate other δ-endotoxins from a mixture of proteins. Specifically, antibodies may be raised to the portions of the δ-endotoxins which are most constant and most distinct from other B. thuringiensis δ-endotoxins. These antibodies can then be used to specifically identify equivalent δ-endotoxins with the characteristic insecticidal activity by immunoprecipitation, enzyme linked immunoassay (ELISA), or Western blotting.
A further method for identifying the δ-endotoxins and genes of the subject invention is through the use of oligonucleotide probes. These probes are nucleotide sequences having a detectable label. As is well known in the art, if the probe molecule and nucleic acid sample hybridize by forming a strong bond between the two molecules, it can be reasonably assumed that the probe and sample are essentially identical. The probe's detectable label provides a means for determining in a known manner whether hybridization has occurred. Such a probe analysis provides a rapid method for identifying formicidal δ-endotoxin genes of the subject invention.
The nucleotide segments which are used as probes according to the invention can be synthesized by use of DNA synthesizers using standard procedures. In the use of the nucleotide segments as probes, the particular probe is labeled with any suitable label known to those skilled in the art, including radioactive and non-radioactive labels. Typical radioactive labels include 32 P, 125 I, 35 S, or the like. A probe labeled with a radioactive isotope can be constructed from a nucleotide sequence complementary to the DNA sample by a conventional nick translation reaction, using a DNase and DNA polymerase. The probe and sample can then be combined in a hybridization buffer solution and held at an appropriate temperature until annealing occurs. Thereafter, the membrane is washed free of extraneous materials, leaving the sample and bound probe molecules typically detected and quantified by autoradiography and/or liquid scintillation counting.
Non-radioactive labels include, for example, ligands such as biotin or thyroxine, as well as enzymes such as hydrolases or peroxidases, or the various chemiluminescers such as luciferin, or fluorescent compounds like fluorescein and its derivatives. The probe may also be labeled at both ends with different types of labels for ease of separation, as, for example, by using an isotopic label at the end mentioned above and a biotin label at the other end.
Duplex formation and stability depend on substantial complementarity between the two strands of a hybrid, and, as noted above, a certain degree of mismatch can be tolerated. Therefore, the probes of the subject invention include mutations (both single and multiple), deletions, insertions of the described sequences, and combinations thereof, wherein said mutations, insertions and deletions permit formation of stable hybrids with the target polynucleotide of interest. Mutations, insertions, and deletions can be produced in a given polynucleotide sequence in many ways, by methods currently known to an ordinarily skilled artisan, and perhaps by other methods which may become known in the future.
The potential variations in the probes listed is due, in part, to the redundancy of the genetic code. Because of the redundancy of the genetic code, i.e., more than one coding nucleotide triplet (codon) can be used for most of the amino acids used to make proteins. Therefore different nucleotide sequences can code for a particular amino acid. Thus, the amino acid sequences of the B. thuringiensis δ-endotoxins and peptides can be prepared by equivalent nucleotide sequences encoding the same amino acid sequence of the protein or peptide. Accordingly, the subject invention includes such equivalent nucleotide sequences. Also, inverse or complement sequences are an aspect of the subject invention and can be readily used by a person skilled in this art. In addition it has been shown that proteins of identified structure and function may be constructed by changing the amino acid sequence if such changes do not alter the protein secondary structure (Kaiser and Kezdy, 1984). Thus, the subject invention includes mutants of the amino acid sequence depicted herein which do not alter the protein secondary structure, or if the structure is altered, the biological activity is substantially retained. Further, the invention also includes mutants of organisms hosting all or part of a δ-endotoxin encoding a gene of the invention. Such mutants can be made by techniques well known to persons skilled in the art. For example, UV irradiation can be used to prepare mutants of host organisms. Likewise, such mutants may include asporogenous host cells which also can be prepared by procedures well known in the art.
Ribozymes are enzymatic RNA molecules which cleave particular mRNA species. In certain embodiments, the inventors contemplate the selection and utilization of ribozymes capable of cleaving the RNA segments of the present invention, and their use to reduce activity of target mRNAs in particular cell types or tissues.
Six basic varieties of naturally-occurring enzymatic RNAs are known presently. Each can catalyze the hydrolysis of RNA phosphodiester bonds in trans (and thus can cleave other RNA molecules) under physiological conditions. In general enzymatic nucleic acids act by first binding to a target RNA. Such binding occurs through the target binding portion of a enzymatic nucleic acid which is held in close proximity to an enzymatic portion of the molecule that acts to cleave the target RNA. Thus, the enzymatic nucleic acid first recognizes and then binds a target RNA through complementary base-pairing, and once bound to the correct site, acts enzymatically to cut the target RNA. Strategic cleavage of such a target RNA will destroy its ability to direct synthesis of an encoded protein. After an enzymatic nucleic acid has bound and cleaved its RNA target, it is released from that RNA to search for another target and can repeatedly bind and cleave new targets.
The enzymatic nature of a ribozyme is advantageous over many technologies, such as antisense technology (where a nucleic acid molecule simply binds to a nucleic acid target to block its translation) since the concentration of ribozyme necessary to affect a therapeutic treatment is lower than that of an antisense oligonucleotide. This advantage reflects the ability of the ribozyme to act enzymatically. Thus, a single ribozyme molecule is able to cleave many molecules of target RNA. In addition, the ribozyme is a highly specific inhibitor, with the specificity of inhibition depending not only on the base pairing mechanism of binding to the target RNA, but also on the mechanism of target RNA cleavage. Single mismatches, or base-substitutions, near the site of cleavage can completely eliminate catalytic activity of a ribozyme. Similar mismatches in antisense molecules do not prevent their action (Woolf et al., 1992). Thus, the specificity of action of a ribozyme is greater than that of an antisense oligonucleotide binding the same RNA site.
The enzymatic nucleic acid molecule may be formed in a hammerhead, hairpin, a hepatitis δ virus, group I intron or RNaseP RNA (in association with an RNA guide sequence) or Neurospora VS RNA motif. Examples of hammerhead motifs are described by Rossi et al. (1 992); examples of hairpin motifs are described by Hampel et al. (Eur. Pat. EP 0360257), Hampel and Tritz (1989), Hampel et a. (1990) and Cech et al. (U.S. Pat. No. 5,631,359; an example of the hepatitis δ virus motif is described by Perrotta and Been (1992); an example of the RNaseP motif is described by Guerrier-Takada et al. (1983); Neurospora VS RNA ribozyme motif is described by Collins (Saville and Collins, 1990; Saville and Collins, 1991; Collins and Olive, 1993); and an example of the Group I intron is described by Cech et al. (U.S. Pat. No. 4,987,071). All that is important in an enzymatic nucleic acid molecule of this invention is that it has a specific substrate binding site which is complementary to one or more of the target gene RNP, regions, and that it have nucleotide sequences within or surrounding that substrate binding site which impart an RNA cleaving activity to the molecule. Thus the ribozyme constructs need not be limited to specific motifs mentioned herein.
The invention provides a method for producing a class of enzymatic cleaving agents which exhibit a high degree of specificity for the RNA of a desired target. The enzymatic nucleic acid molecule is preferably targeted to a highly conserved sequence region of a target mRNA such that specific treatment of a disease or condition can be provided with either one or several enzymatic nucleic acids. Such enzymatic nucleic acid molecules can be delivered exogenously to specific cells as required. Alternatively, the ribozymes can be expressed from DNA or RNA vectors that are delivered to specific cells.
Small enzymatic nucleic acid motifs (e.g., of the hammerhead or the hairpin structure) may be used for exogenous delivery. The simple structure of these molecules increases the ability of the enzymatic nucleic acid to invade targeted regions of the mRNA structure. Alternatively, catalytic RNA molecules can be expressed within cells from eukaryotic promoters (e.g., Scanlon et al., 1991; Kashani-Sabet et al., 1992; Dropulic et al., 1992; Weerasinghe et al., 1991; Ojwang et al., 1992; Chen et al., 1992; Sarver et al., 1990). Those skilled in the art realize that any ribozyme can be expressed in eukaryotic cells from the appropriate DNA vector. The activity of such ribozymes can be augmented by their release from the primary transcript by a second ribozyme (Draper et al., Int. Pat. Appl. Publ. No. WO 93/23569, and Sullivan el al., Int. Pat. Appl. Publ. No. WO 94/02595, both hereby incorporated in their totality by reference herein; Ohkawa et al., 1992; Taira et al., 1991; Ventura et al., 1993).
Ribozymes may be added directly, or can be complexed with cationic lipids, lipid complexes, packaged within liposomes, or otherwise delivered to target cells. The RNA or RNA complexes can be locally administered to relevant tissues ex vivo, or in vivo through injection, aerosol inhalation, infusion pump or sterit, with or without their incorporation in biopolymers.
Ribozymes may be designed as described in Draper et al. (Int. Pat. Appl. Publ. No. WO 93/23569), or Sullivan et al., (Int. Pat. Appl. Publ. No. WO 94/02595) and synthesized to be tested in vitro and in vivo, as described. Such ribozymes can also be optimized for delivery. While specific examples are provided, those in the art will recognize that equivalent RNA targets in other species can be utilized when necessary.
Hammerhead or hairpin ribozymes may be individually analyzed by computer folding (Jaeger et al., 1989) to assess whether the ribozyme sequences fold into the appropriate secondary structure. Those ribozymes with unfavorable intramolecular interactions between the binding arms and the catalytic core are eliminated from consideration. Varying binding arm lengths can be chosen to optimize activity. Generally, at least 5 bases on each arm are able to bind to, or otherwise interact with, the target RNA.
Ribozymes of the hammerhead or hairpin motif may be designed to anneal to various sites in the mRNA message, and can be chemically synthesized. The method of synthesis used follows the procedure for normal RNAk synthesis as described in Usman et al. (1987) and in Scaringe et al. (1990) and makes use of common nucleic acid protecting and coupling groups, such as dimethoxytrityl at the 5'-end, and phosphoramidites at the 3'-end. Average stepwise coupling yields are typically >98%. Hairpin ribozymes may be synthesized in two parts and annealed to reconstruct an active ribozyme (Chowrira and Burke, 1992). Ribozymes may be modified extensively to enhance stability by modification with nuclease resistant groups, for example, 2'-amino, 2'-C-allyl, 2'-flouro, 2'-o-methyl, 2'-H (for a review see Usman and Cedergren, 1992). Ribozymes may be purified by gel electrophoresis using general methods or by high pressure liquid chromatography and resuspended in water.
Ribozyme activity can be optimized by altering the length of the ribozyme binding arms, or chemically synthesizing ribozymes with modifications that prevent their degradation by serum ribonucleases (see e.g., Int. Pat. Appl. Publ. No. WO 92/07065; Perrault et al, 1990; Pieken et al., 1991; Usman and Cedergren, 1992; Int. Pat. Appl. Publ. No. WO 93/15187; Int. Pat. Appl. Publ. No. WO 91/03162; Eur. Pat. Appl. Publ. No. 92110298.4; U.S. Pat. No. 5,334,711; and Int. Pat. Appl. Publ. No. WO 94/13688, which describe various chemical modifications that can be made to the sugar moieties of enzymatic RNA molecules), modifications which enhance their efficacy in cells, and removal of stem II bases to shorten RNA synthesis times and reduce chemical requirements.
Sullivan et al (Int. Pat. Appl. Publ. No. WO 94/02595) describes the general methods for delivery of enzymatic RNA molecules. Ribozymes may be administered to cells by a variety of methods known to those familiar to the art, including, but not restricted to, encapsulation in liposomes, by iontophoresis, or by incorporation into other vehicles, such as hydrogels, cyclodextrins, biodegradable nanocapsules, and bioadhesive microspheres. For some indications, ribozymes may be directly delivered ex vivo to cells or tissues with or without the aforementioned vehicles. Alternatively, the RNA/vehicle combination may be locally delivered by direct inhalation, by direct injection or by use of a catheter, infusion pump or stent. Other routes of delivery include, but are not limited to, intravascular, intramuscular, subcutaneous or joint injection, aerosol inhalation, oral (tablet or pill form), topical, systemic, ocular, intraperitoneal and/or intrathecal delivery. More detailed descriptions of ribozyme delivery and administration are provided in Sullivan et al. (Int. Pat. Appl. Publ. No. WO 94/02595) and Draper et al (Int. Pat. Appl. Publ. No. WO 93/23569) which have been incorporated by reference herein.
Another means of accumulating high concentrations of a ribozyme(s) within cells is to incorporate the ribozyme-encoding sequences into a DNA expression vector. Transcription of the ribozyme sequences are driven from a promoter for eukaryotic RNA polymerase I (pol I), RNA polymerase II (pol II), or RNA polymerase III (pol III). Transcripts from pol I or pol III promoters will be expressed at high levels in all cells; the levels of a given pol II promoter in a given cell type will depend on the nature of the gene regulatory sequences (enhancers, silencers, etc.) present nearby. Prokaryotic RNA polymerase promoters may also be used, providing that the prokaryotic RNA polymerase enzyme is expressed in the appropriate cells (Elroy-Stein and Moss, 1990; Gao and Huang, 1993; Lieber et al., 1993; Zhou et al., 1990). Ribozymes expressed from such promoters can function in mammalian cells (e.g. Kashani-Saber et al., 1992; Ojwang et al., 1992; Chen et al., 1992; Yu et al., 1993; L'Huillier et al., 1992; Lisziewicz et al., 1993;). Such transcription units can be incorporated into a variety of vectors for introduction into mammalian cells, including but not restricted to, plasmid DNA vectors, viral DNA vector, (such as adenovirus or adeno-associated vectors), or viral RNA vectors (such as retroviral, semliki forest virus, sindbis virus vectors).
Ribozymes of this invention may be used as diagnostic tools to examine genetic drift and mutations within cell lines or cell types. They can also be used to assess levels of the target RNA molecule. The close relationship between ribozyme activity and the structure of the target RNA allows the detection of mutations in any region of the molecule which alters the base-pairing and three-dimensional structure of the target RNA. By using multiple ribozymes described in this invention, one may map nucleotide changes which are important to RNA structure and function in vitro, as well as in cells and tissues. Cleavage of target RNAs with ribozymes may be used to inhibit gene expression and define the role (essentially) of specified gene products in particular cells or cell types.
The following examples are included to demonstrate preferred embodiments of the invention. It should be appreciated by those of skill in the art that the techniques disclosed in the examples which follow represent techniques discovered by the inventor to function well in the practice of the invention, and thus can be considered to constitute preferred modes for its practice. However, those of skill in the art should, in light of the present disclosure, appreciate that many changes can be made in the specific embodiments which are disclosed and still obtain a like or similar result without departing from the spirit and scope of the invention.
Three-Dimensional Structure of Cry3Bb
The three-dimensional structure of Cry3Bb was determined by X-ray crystallography. Crystallization of Cry3Bb and X-ray diffraction data collection were performed as described by Cody et al. (1992). The crystal structure of Cry3Bb was refined to a residual R factor of 18.0% using data collected to 2.4 Å resolution. The crystals belong to the space group C2221 with unit cell dimensions a=122.44, b=131.81, and c=105.37 Å and contain one molecule in the asymmetric unit. Atomic coordinates for Cry3Bb are described in Example 31 and listed in Section 9.
The structure of Cry3Bb is similar to that of Cry3A (Li et al., 1991). It consists of 5825 protein atoms from 588 residues (amino acids 64-652) forming three discrete domains (FIG. 1). A total of 251 water molecules have been identified in the Cry3Bb structure (FIG. 2). Domain 1 (residues 64-294) is a seven helical bundle formed by six helices twisted around the central helix, α5 (FIG. 3). The amino acids forming each helix are listed in FIG. 4. Domain 2 (residues 295-502) contains three antiparallel β-sheets (FIG. 5A and FIG. 5B). Sheets 1 and 2, each composed of 4β strands, form the distinctive "Greek key" motif. The outer surface of sheet 3, composed of 3β strands, makes contact with helix α7 of domain 1. FIG. 6 lists the amino acids comprising each β strand in domain 2. A small α helix, α8 which follows β strand 1, is also included in domain 2. Domain 3 (residues 503-652) has a "jelly roll" β-barrel topology which has a hydrophobic core and is nearly parallel to the a and perpendicular to the c axes of the lattice (FIG. 7A and FIG. 7B). The amino acids comprising each β strand of domain 3 are listed in FIG. 8.
The monomers of Cry3Bb in the crystal form a dimeric quaternary structure along a two-fold axis parallel to the a axis (FIG. 9A and FIG. 9B). Helix α6 lies in a cleft formed by the interface of domain 1 and domains 1 and 3 of its symmetry related molecule. There are numerous close hydrogen bonding contacts along this surface, confirming the structural stability of the dimer.
Preparation of Cry3Bb.60
B. thuringiensis EG7231 was grown through sporulation in C2 medium with chloramphenicol (Cml) selection. The solids from this culture were recovered by centrifugation and washed with water. The toxin was purified by recrystallization from 4.0 M NaBr (Cody et al, 1992). The purified Cry3Bb was solubilized in 10 ml of 50mM KOH/100 mg Cry3Bb and buffered to pH 9.0 with 100 mM CAPS (pH 9.0). The soluble toxin was treated with trypsin at a weight ratio of 50 mg toxin to 1 mg trypsin. After 20 min of trypsin digestion the predominant protein visualized by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) was 60 kDa. Further digestion of the 60-kDa toxin was not observed. FIG. 4 illustrates the Coomassie-stained Cry3Bb and Cry3Bb.60 following SDS-PAGE.
Purification and Sequencing of Cry3Bb.60
Cry3Bb.60 was electrophoretically purified by SDS-PAGE and electroblotted to Immobilon-® (Millipore) membrane by semi-dry transfer at 15V for 30 min. The membrane was then washed twice with water and stained with 0.025% R-250, 40% methanol. To reduce the background, the blot was destained with 50% methanol until the stained protein bands were visible. The blot was then air dried, and the stained Cry3Bb.60 band was cut out of the membrane. This band was sent to the Tufts University Sequencing Laboratory (Boston, Mass.) for N-terminal sequencing. The experimentally-determined N-terminal amino acid sequence is shown in Table 7 beside the known amino acid sequence starting at amino acid residue 160.
TABLE 7
______________________________________
AMINO ACID SEQUENCE OF THE N-TERMINUS OF CRY3BB.60
AND COMPARISON TO THE KNOWN SEQUENCE OF CRY3BB
Deduced Sequence
Known Sequence
Residue #
______________________________________
S S 160
K K 161
R R 162
S S 163
Q Q 164
D D 165
R R 166
______________________________________
Bioactivity of Cry3Bb.60
Cry3Bb was prepared for bioassay by solubilization in a minimal amount of 50 mM KOH, 10 ml per 100 mg toxin, and buffered to pH 9.0 with 100 mM CAPS, pH 9.0. Cry3Bb.60 was prepared as described in Example 1. Both preparations were kept at room temperature 12 to 16 hours prior to bioassay. After seven days the mortality of the population was determined and analyzed to determine the lethal concentration of each toxin. These results are numerized in Table 8.
TABLE 8
______________________________________
BIOACTIVITY OF CRY3BB AND CRY3BB.60 AGAINST THE
SOUTHERN CORN ROOTWORM
(DIABIOTICA UNDECIMPUNCTATA)
LC.sub.50 mg/well
95% C. I.
______________________________________
Cry3Bb 24.09 15-39
Cry3Bb.60 6.72 5.25-8.4
______________________________________
Ion-Channel Formation by Cry3Bb and CRYB2.60
Cry3Bb.60 and Cry3Bb were evaluated for their ability to form ion channels in planar lipid bilayers. Bilayers of phosphatidylcholine were formed on Teflon® supports over a 0.7-mm hole. A bathing solution of 3.5 ml 100 mM KOH, 10 mM CaCl2, 100 mM CAPS (pH 9.5) was placed on either side of the Teflon® partition. The toxin was added to one side of the partition and a voltage of 60 mV was imposed across the phosphatidylcholine bilayer. Any leakage of ions through the membrane was amplified and recorded. An analysis of the frequency of the conductances created by either Cry3Bb or Cry3Bb.60 are illustrated in FIG. 5A and FIG. 5B. Cry3Bb.60 readily formed ion channels whereas Cry3Bb rarely formed channels.
Formation of High Molecular-Weight Oligomers
Individual molecules of Cry3Bb or Cry3Bb.60 form a complex with another like molecule. The ability of Cry3Bb to form an oligomer is not reproducibly apparent. The complex cannot be repeatedly observed to form under nondenaturing conditions. Cry3Bb.60 formed a significantly greater amount of a higher molecular-weight complex (≧120 kDa) with other Cry3Bb.60 molecules. Oligomers of Cry3Bb are demonstrated by the intensity of the Coomassie-stained SDS polyacrylamide gel. Oligomerization is visualized on SDS-PAGE by not heating samples prior to loading on the gel to retain some nondenatured toxin. These data suggest that Cry3Bb.60 more readily forms the higher order complex than Cry3Bb alone. Oligomerization is also observed by studying the conductance produced by these molecules and the time-dependent increase in conductance. This change in conductance can be attributed to oligomerization of the toxin.
Design Method 1: Identification and Alteration of Protease-Sensitive Sites and Proteolytic Processing
It has been reported in the literature that: treatment of Cry3A toxin protein with trypsin, an enzyme that cleaves proteins on the carboxyl side of available lysine and arginine residues, yields a stable cleavage product of 55 kDa from the 67 kDa native protein (Carroll et al., 1989). N-terminal sequencing of the 55 kDa product showed cleavage occurs at amino acid residue R158. The truncated Cry3A protein was found to retain the same level of insecticidal activity as the native protein. Cry3Bb toxin protein was also treated with trypsin. After digestion, the protein size decreased from 68 kDa, the molecular weight of the native Cry3Bb toxin, to 60 kDa. No further digestion was observed. N-terminal sequencing revealed the trypsin cleavage site of the truncated toxin (Cry3Bb.60) to be amino acid R159 in lα3,4 of Cry3Bb. Unexpectedly, the bioactivity of the truncated Cry3Bb toxin was found to increase.
Using this method, protease digestion of a B. thuringiensis toxin protein, a proteolytically sensitive site was identified on Cry3Bb, and a more highly active form of the protein (Cry3Bb.60) was identified. Modifications to this proteolytically-sensitive site by introducing an additional protease recognition site also resulted in the isolation of a biologically more active protein. It is also possible that removal of other protease-sensitive site(s) may improve activity. Proteolytically sensitive regions, once identified, may be modified or utilized to produce biologically more active toxins.
Treatment of solubilized Cry3Bb toxin protein with trypsin results in the isolation of a stable, truncated Cry3Bb toxin protein with a molecular weight of 60 kDa (Cry3Bb.60). N-terminal sequencing of Cry3Bb.60 shows the trypsin-sensitive site to be R159 in lα3,4 of the native toxin. Trypsin digestion results in the removal of helices 1-3 from the native Cry3Bb but also increases the activity of the toxin against SCRW larvae approximately four-fold.
Cry3Bb.60 is a unique toxin with enhanced insecticidal use over the parent Cry3Bb. Improved biological activity, is only one parameter that distinguishes it as a new toxin. Aside from the reduced size, Cry3Bb.60 is also a more soluble protein. Cry3Bb precipitates from solution at pH 6.5 while Cry3Bb.60 remains in solution from pH 4.5 to pH 12. Cry3Bb.60 also forms ion channels with greater frequency than Cry3Bb.
Cry3Bb.60 is produced by either the proteolytic removal of the first 159 amino acid residues, or the in vivo production of this toxin, by bacteria or plants expressing the gene for Cry3Bb.60, that is, the Cry3Bb gene without the first 483 nucleotides.
In conclusion, Cry3Bb.60 is distinct from Cry3Bb in several important ways: enhanced insecticidal activity; enhanced range of solubility; enhanced ability to form channels; and reduced size.
Semi-random mutagenesis of the trypsin-sensitive lα3,4 region of Cry3Bb resulted in the isolation of Cry3Bb.11221, a designed Cry3Bb protein that exhibits over a 6-fold increase in activity against SCRW larvae compared to WT. Cry3Bb.11221 has 4 amino acid changes in the lα3,4 region. One of these changes, L158R, introduces an additional trypsin site adjacent to R159, the proteolytically sensitive site used to produce Cry3Bb.60 (example 4.1.1). Cry3Bb.11221 is produced by B. thuringiensis as a full length toxin protein but is presumably digested by insect gut proteases to the same size as Cry3Bb.60 (see Cry3A results from Carroll et al., 1989). The additional protease recognition site may make the lα3,4 region even more sensitive to digestion, thereby increasing activity.
Design Method 2: Determination and Manipulation of Bound Water
There are several ways that water molecules can associate with a protein, including surface water that is easily removed and bound water that is more difficult to extract (Dunitz, 1994; Zhang and Matthews, 1994). The function of bound water has been the subject of significant academic extrapolation, but the precise function has little experimental validation. Some of the most interesting bound or structural water is the water that participates in the protein structure from inside the protein itself.
The occupation of a site by a water molecule can indicate a stable pocket within a protein or a looseness of packing created by water-mediated salt bridges and hydrogen bonding to water. This can reduce the degree of bonding between amino acids, possibly making the region more flexible. A different amino acid sequence around that same site could result in better packing, collapsing the pocket around polar or charged amino acids. This may result in decreased flexibility. Therefore, the degree of hydration of a region of a protein may determine the flexibility or mobility of that region, and manipulation of the hydration may alter the flexibility. Methods of increasing the hydration of a water-exposed region include increasing the number of hydrophobic residues along that surface. It is taught in the art that exposed hydrophobic residues require significantly more water to hydrate than hydrophilic residues (CRC Handbook of Chemistry and Physics, CRC Press, Inc.). It is not taught, however, that by doing this, improvements to the biological activity of a protein can be achieved.
Structural water has not previously been identified in B. thuringiensis δ-endotoxins including Cry3Bb. Furthermore, there are no reports of the function of this structural water in δ-endotoxins or bacterial toxins. In the analysis of Cry3Bb, it was observed that a collection of water molecules are located around lα3,4, a site defined by the inventors as important for improvement of bioactivity. The loop α3,4 region is surface exposed and may define a hinge in the protein permitting either removal or movement of the first three helices of domain 1. The hydration found around this region may impart flexibility and mobility to this loop. The observation of structural water at the lα3,4 site provided an analytical tool for further structure analysis. If this important site is surrounded by water, then other important sites may also be completely or partially surrounded by water. Using this insight, structural water surrounding helices 5 and 6 was then identified. This structural water forms a column through the protein, effectively separating helices 5 and 6 from the rest of the molecule. The structures of Cry3A and Cry3Bb suggest that helices 5 and 6 are tightly associated, bound together by Van der Waals interactions. Alone, helix 5 from Cry3A, although insufficient for biological activity, has been demonstrated to have the ability to form ion channels in an artificial membrane (Gazit and Shai, 1993). The ion channels formed by helix 5 are 10-fold smaller than the channels of the full length toxin suggesting that significantly more toxin structure is required for the full-sized ion channels. In Cry3Bb, helix 5 as part of a cluster of α helices (domain 1) has been found to form ion channels (Von Tersch et al., 1994). Unpublished experimental observations by the inventors demonstrate that helix 6 also crossed the biological membrane. Helices 5 and 6, therefore, are the putative channel-forming helices necessary for toxicity.
The hydration around these helices may indicate that flexibility of this region is necessary for toxicity. It is conceivable, therefore, that if it were possible to improve the hydration around helices 5 and 6, one could create a better toxin protein. Care must be taken, however, to avoid creating continuous hydrophobic surfaces between helices 5-6 and any other part of the protein which could, by hydrophobic interactions, act to restrict movement of the mobile helices. The mobility of helices 5 and 6 may also depend on the flexibility of the loops attached to them as well as on other regions of the Cry3Bb molecule, particularly in domain 1, which may undergo conformational changes to allow insertion of the 2 helices into the membrane. Altering the hydration of these regions of the protein may also affect its bioactivity.
A collection of bound water residues indicated the relative flexibility of the lα3,4 region. The flexibility of this loop can be increased by increasing the hydration of the region by substituting relatively hydrophobic residues for the exposed hydrophilic residues. An example of an improved, designed protein having this type of substitution is Cry3Bb.11032. Cry3Bb.11032 has the amino acid change D165G; glycine is more hydrophobic than aspartate (Kyte and Doolittle hydrophobicity score of -0.4 vs. -3.5 for aspartate). Cry3Bb.11032 is approximately 3 times more active than WT Cry3Bb.
To increase the hydration of the lα4,5 region of Cry3Bb, glycine was substituted for the surface exposed residue K189. Glycine is more hydrophobic than lysine (Kyte and Doolittle hydrophobicity score of -0.4 vs. -3.9 for lysine) and may result in an increase in bound water. The increase in bound water may impart greater flexibility to the loop region which precedes the channel-forming helix, α5. The designed Cry3Bb protein with the K189G change, Cry3Bb.11051, exhibits a 3-fold increase in activity compared to WT Cry3Bb.
Amino acid changes made in the surface-exposed loop connecting α-helix 7 and β-strand 1 (lα7,β1) resulted in the identification of 2 altered Cry3Bb proteins with increased bioactivities, Cry3Bb.11241 and Cry3Bb.11242. Analysis of the hydropathy index of 2 of these proteins over the 20 amino acid sequence 281-300, inclusive of the lα7,β1 region, reveal that the amino acid substitutions in these proteins have made the lα7,β1 region much more hydrophobic. The grand average of hydropathy value (GRAVY) was determined for each protein sequence using the PC\GENE® (IntelliGenetics, Inc., Mountain View, Calif., release 6.85) protein sequence analysis computer program, SOAP, and a 7 amino acid interval. The SOAP program is based on the method of Kyte and Doolittle (1982). The increase in hydrophobicity of the lα7,β1 region for each protein may increase the hydration of the loop and, therefore, the flexibility. The altered proteins, their respective amino acid changes, fold-increases over WT bioactivity, and GRAVY values are listed in Table 9.
TABLE 9
__________________________________________________________________________
HYDROPATHY VALUES FOR THE Lα7,β1 REGION OF CRY3BB AND 2
DESIGNED CRY3BB PROTEINS SHOWING INCREASED SCRW BIOACTIVITY
Fold Increase in
GRAVY
Cry3Bb* Bioactivity Over
(Amino Acids 281-
Protein Amino Acid Changes
WT 300)
__________________________________________________________________________
wildtype
-- -- 4.50
Cry3Bb.11241
Y287F, D288N, R290L
2.6x 10.70
Cry3Bb.11242
R290V 2.5x 8.85
__________________________________________________________________________
The surface-exposed loop between β-strand 1 and α-helix 8 (lβ1,α8) defines the boundary between domains 1 and 2 of Cry3Bb. The introduction of semi-random amino acid changes to this region resulted in the identification of several altered Cry3Bb proteins with increased bioactivity. Hydropathy index analysis of the amino acid substitutions found in the altered proteins shows that the changes have made the exposed region more hydrophobic which may result in increased hydration and flexibility. Table 10 lists the altered proteins, their respective amino acid changes and fold increases over WT Cry3Bb and the grand average of hydropathy value (GRAVY) determined using the PC\GENE® (IntelliGenetics, Inc., Mountain View, Calif., release 6.85) protein sequence analysis program, SOAP, over the 20 amino acid sequence 305-324 inclusive of lβ1,α8, using a 7 amino acid interval.
TABLE 10
______________________________________
HYDROPATHY VALUES FOR THE Lβ1,α8 REGION
OF CRY3BB AND 8 DESIGNED CRY3BB*
PROTEINS SHOWING INCREASED SCRW BIOACTIVITY
Fold Increase in
GRAVY
Cry3Bb* Amino Acid Bioactivity Over
(Amino Acids
Protein Changes Wild Type 305-324)
______________________________________
wildtype -- -- 0.85
Cry3Bb.11228
S311L, N313T,
4.1× 4.35
E317K
Cry3Bb.11229
S311T, E317K,
2.5× 2.60
Y318C
Cry3Bb.11230
S311A, L312V,
4.7× 3.65
Q316W
Cry3Bb.11233
S311A, Q316D
2.2× 2.15
Cry3Bb.11236
S311I 3.1× 3.50
Cry3Bb.11237
S311I, N313H
5.4× 3.65
Cry3Bb.11238
N313V, T314N,
2.6× 9.85
Q316M, E317V
Cry3Bb.11239
N313R, L315P,
2.8× 3.95
Q316L, E317A
______________________________________
Amino acid Q238, located in helix 6 of Cry3Bb, has been identified as a residue that, by its large size and hydrogen bonding to R290, blocks complete hydration of the space between helix 6 and helix 4. Substitution of R290 with amino acids that do not form hydrogen bonds or that have side chains that can not span the physical distance to hydrogen bond with Q238 may result in increased hydration around Q238. Q238, unable to hydrogen bond to R-290, may now bind water. This may increase the flexibility of the channel-forming region. Designed proteins Cry3Bb.11227 (R290N), Cry3Bb.11241 (R290L) and Cry3Bb.11242 (R290V) show increased activities of approximately 2-fold, 2.6-fold and 2.5-fold, respectively, against SCRW larvae compared to WT.
Design Method 3: Manipulation of Hydrogen Bonds Around Mobile Regions
Mobility of regions of a protein may be required for activity. The mobility of the α5,6 region, the putative channel-forming region of Cry3Bb, may be improved by decreasing the number of hydrogen bonds, including salt bridges (hydrogen bonds between oppositely charged amino acid side chains), between helices 5-6 and any other part of the molecule or dimer structure. These hydrogen bonds may impede the movement of the two helices. Decreasing the number of hydrogen bonds and salt bridges may improve biological activity. Replacement of hydrogen-bonding amino acids with hydrophobic residues must be done with caution to avoid creating continuous hydrophobic surfaces between helices 5-6 and any other part of the dimer. This may decrease mobility by increasing hydrophobic surface interactions.
Tyr230 is located on helix 6 and, in the quaternary dimer structure of Cry3Bb, this amino acid is coordinated with Tyr230 from the adjacent molecule. Three hydrogen bonds are formed between the two helices 6 in the two monomers because of this single amino acid. In order to improve the flexibility of helices 5-6, the helices theoretically capable of penetrating the membrane and forming an ion channel, the hydrogen bonds across the dimer were removed by changing this amino acid and a corresponding increase in biological activity was observed. The designed Cry3Bb proteins, Cry3Bb.11222 and Cry3Bb.EG11223, show a 4-fold and 2.8-fold increase in SCRW activity, respectively, compared to WT.
Designed Cry3Bb protein Cry3Bb.11051 has amino acid change K189G in lα4,5 of domain 1. In the WT Cry3Bb structure, the exposed side chain of K189 is close enough to the exposed side change of E123, located in lα2b,3, to form hydrogen bonds. Substitution of K189 with glycine, as found in this position in Cry3A, removes the possibility of hydrogen bond formation at this site and results in a protein with a bioactivity three-fold greater than WT Cry3Bb.
Amino acid Q238, located in helix 6 of Cry3Bb, has been identified as a residue that, by its large size and hydrogen bonding to R290, blocks complete hydration of the space between helix 6 and helix 4. Substitution of R290 with amino acids that do not form hydrogen bonds or that have side chains that can not span the physical distance to hydrogen bond with Q238 may increase the flexibility of the channel-forming region. Designed proteins Cry3Bb.11227 (R290N), Cry3Bb.11241 (R290L) and Cry3Bb.11242 (R290V) show increased activities of approximately 2-fold, 2.6-fold and 2.5-fold, respectively, against SCRW larvae compared to WT
Design Method 4: Loop Analysis and Loop Design Around Flexible Helices
Loop regions of a protein structure may be involved in numerous functions of the protein including, but not limited to, channel formation, quaternary structure formation and maintenance, and receptor binding. Cry3Bb is a channel-forming protein. The availability of the ion channel-forming helices of δ-endotoxins to move into the bilayer depend upon the absence of forces that hinder the process. One of the forces possibly limiting this process is the steric hindrance of amino acid side chains in loop) regions around the critical helices. The literature suggests that in at least one other bacterial toxin, not a B. thuringiensis toxin, the toxin molecule opens up or, in scientific terms, loses some of the quaternary structure to expose a membrane-active region (Cramer et al., 1990). This literature does not teach how to improve the probability of this event occurring and it is not known if B. thuringiensis toxins use this same process to penetrate the membrane. Reducing the steric hindrance of the amino acid side chains in these critical regions by reducing size or altering side chain positioning with the corresponding increase in biological activity was the inventive step.
The inventors have discovered that the first three helices of domain one could be cleaved from the rest of the toxin by proteolytic digestion of the loop between helices α3 and α4 (Cry3Bb.60). Initial efforts to truncate the cry3Bb gene to produce this shortened, though more active Cry3Bb molecule, failed. For unknown reasons, B. thuringiensis failed to synthesize this 60-kDa molecule. It was then reasoned that perhaps the first three helices of domain 1 did not have to be proteolytically removed, or equivalently, the protein did not have to be synthesized in this truncated form to take advantage of the Cry3Bb.60 design. It was observed that the protein Cry3A had a small amino acid near the lα3,4 that might impart greater flexibility in the loop region thereby permitting the first three helices of domain 1 to move out of the way, exposing the membrane-active region. By designing a Cry3Bb molecule with a glycine residue near this loop, the steric hindrance of residues in the loop might be lessened. The redesigned protein, Cry3Bb.11032, has the amino acid change D165G, which replaces the larger aspartate residue (average mass of 115.09) with the smallest amino acid, glycine (average mass of 57.05). The activity of Cry3Bb.11032 is approximately 3-fold greater than that of the WT protein. In this way, the loop between helices α3 and α4 was rationally redesigned with a corresponding increase in the biological activity.
The loop region connecting helices α4 and α5 in Cry3Bb must be flexible so that the channel-forming helices α5-α6 can penetrate into the membrane. It was noticed that Cry3A has a glycine residue in the middle of this loop that may impart greater flexibility. The corresponding change, K189G, was made in Cry3Bb and the resulting, designed protein, Cry3Bb.11051, exhibits a 3-fold increase in activity against SCRW larvae compare to WT Cry3Bb. 5.10.3 Analysis of the Loop Between β-Strand 1 and Helix 8 (Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, AND Cry3Bb.11239)
The loop region located between β strand 1 of domain 2 and α helix 8 in domain 2 is very close to the loop between cc helices 6 and 7 in domain 1. Some of the amino acids side chains of lβ1, α8 appear as though they may sterically impede movement of lα6,7. Since lα6,7 must be flexible for the channel-forming helices α5-α6 to insert into the membrane, it was thought that re-engineering this loop may change the positioning of the side chains resulting in less steric hindrance. This was accomplished creating proteins with increased biological activities ranging from 2.2 to 5.4 times greater than WT. These designed toxin proteins and their amino acid changes are listed in Table 2 as Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11232, Cry3Bb.112313, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, and Cry3Bb.11239.
If Cry3Bb is similar to a bacterial toxin which must open up to expose a membrane active region for toxicity, it is possible that other helices in addition to the channel-forming helices must also change positions. It was reasoned that, if helices α5-α6 insert into the membrane, than helix α7 may have to change positions also. It was shown in example 4.4.3 that increasing flexibility between helix α6 and α7 can increase activity, greater flexibility in the loop following helix α7,lα7,β1 may also increase bioactivity. Alterations to the lα7,β1 region of Cry3Bb resulted in the isolation of several proteins with increased activities ranging from 1.9 to 4.3 times greater than WT. These designed proteins are listed in Table 7 as Cry3Bb.11227, Cry3Bb.11234, Cry3Bb.11241, Cry3Bb.11242, and Cry3Bb.11036.
Design Method 5: Loop Design Around β Strands and β Sheets
Loop regions of a protein structure may be involved in numerous functions of the protein including, but not limited to, channel formation, quaternary structure formation and maintenance, and receptor binding. A binding surface is often defined by a number of loops, as is the case with immunoglobulin G (IgG) (sec Branden and Tooze, 1991, for review). What can not be determined at this point, however, is what loops will be important for receptor interactions just by looking at the structure of the protein in question. Since a receptor has not been identified for Cry3Bb, it is not even possible to compare the structure of Cry3Bb with other proteins that have the same receptor for structural similarities. To identify Cry3Bb loops that contribute to receptor interactions, random mutagenesis was performed on surface-exposed loops.
As each loop was altered, the profile of the overall bioactivities of the resultant proteins were examined and compared. The loops, especially in domain 2 which appears to be unnecessary for channel activity, fall into two categories: (1) loops that could be altered without much change in the level of bioactivity of the resultant proteins and (2) loops where alterations resulted in overall loss of resultant protein bioactivity. Using this design method, it is possible to identify several loops important for activity.
Semi-random mutagenesis of the loop region between β strands 2 and 3 resulted in the production of structurally stable toxin proteins with significantly reduced activities against SCRW larvae. The lβ2,3 region is highly sensitive to amino acid changes indicating that specific amino acids or amino acid sequences ate necessary for toxin protein activity. It is conceivable, therefore, that specific changes in the lβ2,3 region will increase the binding and, therefore, the activity of the redesigned toxin protein.
Semi-random mutations introduced to the loop region between β strands 6 and 7 resulted in structurally stable proteins with an overall loss of SCRW bioactivity. The lβ6,7 region is highly sensitive to amino acid changes indicating that specific amino acids or amino acid sequences are necessary for toxin protein activity. It is conceivable, therefore, that specific changes in the lβ6.7 region will increase the binding and, therefore, the activity of the redesigned toxin protein.
Random mutations to the loop region between β strands 10 and 11 resulted in proteins having an overall loss of SCRW bioactivity. Loop β10,11 is structurally close to and interacts with loops β2,3 and β6,7. Specific changes to individual residues within the lβ10,11 region may also result in increased interaction with the insect membrane, increasing the bioactivity of the toxin protein.
Loops β2,3, β6,7 and β10,11 have been identified as important for bioactivity of Cry3Bb. The 3 loops are surface-exposed and structurally close together. Amino acid Q348 in the WT structure, located in β-strand 2 just prior to lβ2,3, does not form any intramolecular contacts. However, replacing Q348 with arginine (Q348R) results in the formation of 2 new hydrogen-bonds between R348 and the backbone carbonyls of R487 and R488, both located in lβ10,11. The new hydrogen bonds may act to stabilize the structure formed by the 3 loops. The designed protein carrying this change, Cry3Bb.11095, is 4.6-fold more active than WT Cry3Bb.
Design Method 6: Identification and Re-Design of Complex Electrostatic Surfaces
Interactions of proteins include hydrophobic interactions (e.g., Van der Waals forces), hydrophilic interactions, including those between opposing charges on amino acid side chains (salt bridges), and hydrogen bonding. Very little is known about δ-endotoxin and receptor interactions. Currently, there are no literature reports identifying the types of interactions that predominate between B. thuringiensis toxins and receptors.
Experimentally, however, it is important to increase the strength of the B. thuringiensis toxin-receptor interaction and not permit the precise determination of the chemical interaction to stand in the way of improving it. To accomplish this, the electrostatic surface of Cry3Bb was defined by solving the Poisson-Boltzman distribution around the molecule. Once this electrically defined surface was solved, it could then be inspected for regions of greatest diversity. It was reasoned that these electrostatically diverse regions would have the greatest probability of participating in the specific interactions between the B. thuringiensis toxin proteins and the receptor, rather than more general and non-specific interactions. Therefore, these regions were chosen for redesign, continuing to increase the electrostatic diversity of the regions. In addition, examination of the electrostatic interaction around the putative channel forming region of the toxin created insights for redesign. This includes identification of an electropositive residue in an otherwise negatively charged conduit (see example 4.6.1).
Examination of the Cry3Bb dimer interface along the domain 1 axis suggested that a pore or conduit for cations might be formed between the monomers. Electrostatic examination of this axis lent additional credibility to this suggestion. In fact, the hypothetical conduit is primarily negatively charged, an observation consistent with the biophysical analysis of cation-selective, δ-endotoxin channels. If a cation channel were formed along the axis of the dimer, then the cation could move between the monomers relatively easily with only one significant hurdle. A positively charged arginine residue (R290) lies in the otherwise negatively charged conduit. This residue could impede the cation movement through the channel. Based on this analysis, R290 was changed to uncharged residues. The bioactivity of redesigned proteins Cry3Bb.11227 (R290N), Cry3Bb.11241 (R290L) and Cry3Bb.11242 (R290V) was improved approximately 2-fold, 2.6-fold and 2.5-fold, respectively.
Trypsin digestion of solubilized Cry3Bb yields a stable, truncated protein with a molecular weight of 60 kDa (Cry3Bb.60). Trypsin digestion occurs on the carboxyl side of residue R159, effectively removing helices 1 through 3 from the native Cry3Bb structure. The cleavage of the first 3 helices exposes an electrostatic surface different than those found in the native structure. The new surface has a combination of hydrophobic, polar and charged characteristics that may play a role in membrane interactions. The bioactivity of Cry3Bb.60 is 3.6-fold greater than that of WT Cry3Bb.
Design Method 7: Identification and Removal of Metal Binding Sites
The literature teaches that the in vitro behavior of B. thuringiensis toxins can be increased by chelating divalent cations from the experimental system (Crawford and Harvey 1988). It was not known, however, how these divalent cations inhibited the in vitro activity. Crawford and Harvey (1988) demonstrated that the short circuit current across the midgut was more severely inhibited by B. thuringiensis in the presence of EDTA, a chelator of divalent ions, than in the absence of this agent, thus suggesting that this step in the mode of action of B. thuringiensis could be potentiated by removing divalent ions. Similar observations were made using black-lipid membranes and measuring an increase in the current created by the δ-endotoxins in the presence of EDTA to chelate divalent ions. There were at least three possible explanations for these observations. The first explanation could be that the divalent ions are too large to move through a ion channel more suitable for monovalent ions, thereby blocking the channel. Second, the divalent ions may cover the protein in the very general way, thereby buffering the charge interactions required for toxin membrane interaction and limiting ion channel activity. The third possibility is that a specific metal binding site exists on the protein and, when occupied by divalent ions, the performance of the ion channel is impaired. Although the literature could not differentiate the value of one possibility over another, the third possibility led to an analysis of the Cry3Bb structure searching for a specific metal binding site that might alter the probability that a toxin could form an ion channel.
A putative metal binding site is formed in the Cry3Bb dimer structure by the H231 residues of each monomer. The H231 residues, located in helix α6, lie adjacent to each other and close to the axis of symmetry of the dimer. Removal of this site by replacement of histidine with other amino acids was evaluated by the absence of EDTA-dependent ion channel activity. The bioactivities of the designed toxin proteins, Cry3Bb.11222, Cry3Bb.11224, Cry3Bb.11225 and Cry3Bb.11226, are increased 4-, 5-, 3.6- and 3-fold, respectively, over that of WT Cry3Bb. Their respective amino acid changes are listed in Table 2.
Design Method 8: Alteration of Quaternary Structure
Cry3Bb can exist in solution as a dimer similar to a related protein, Cry3A (Walters et al., 1992). However, the importance of the dimer to biological activity is not known because the toxin as a monomer or as a higher order structure has not been seriously evaluated. It is assumed that specific amino acid residues contribute to the formation and stability of the quaternary structure. Once a contributing residue is identified, alterations can be made to diminish or enhance the effect of that residue thereby affecting the interaction between monomers. Channel activity is a useful way, but by no means the only way, to assess quaternary structure of Cry3Bb and its derivatives. It has been observed that Cry3Bb creates gated conductances in membranes that grow in size with time, ultimately resulting in large pores in the membrane (the channel activity of WT Cry3Bb is described in Section 12.1). It also has been observed that Cry3A forms a more stable dimer than Cry3Bb and coincidentally forms higher level conductances faster (FIG. 10). This observation led the inventors to propose that oligomerization and ion channel formation (conductance size and speed of channel formation) were related. Based on this observation Cry3Bb was reengineered to make larger and more stable oligomers at a faster rate. It is assumed in this analysis that the rate of ion channel formation and growth mirrors this process. It is also possible that changes in quaternary structure may not affect channel activity alone or at all. Alterations to quaternary structure may also affect receptor interactions, protein processing in the insect gut environment, as well as other aspects of bioactivity unknown.
Comparative structural analysis of Cry3A and Cry3Bb led to the identification of structural differences between the two toxins in the ion channel-forming domain; specifically, an insertion of one amino acid between helix 2a and helix 2b in Cry3Bb. Removal of this additional amino acid in Cry 3B2, A104, and a D103E substitution, as in Cry3A, resulted in loss of channel gating and the formation of symmetrical pores. Once the pores are formed they remain open and allow a steady conductance ranging from 25-130 pS. This designed protein, Cry3Bb.11048, is 4.3 times more active than WT Cry3Bb against SCRW larvae.
Individual molecules of Cry3Bb or Cry3Bb.60 can form a complex with another like molecule. Oligomerization of Cry3Bb is demonstrated by SDS-PAGE, where samples are not heated in sample buffer prior to loading on the gel. The lack of heat treatment allows some nondenatured toxin to remain. Oligomerization is visualized following Coomassie staining by the appearance of a band at 2 times the molecular weight of the monomer. The intensity of the higher molecular weight band reflects the degree of oligomerization. The ability of Cry3Bb to form an oligomer is not reproducibly apparent. The complex cannot be repeatedly observed to form. Cry3Bb.60, however, forms a significantly greater amount of a higher molecular weight complex (120 kDa). These data suggest that Cry3Bb.60 more readily forms the higher order complex than Cry3Bb alone. Cry3Bb.60 also forms ion channels with greater frequency than WT Cry3Bb (see Section 5.12.9).
Changes were made in Cry3Bb to reflect the amino acid sequence in Cry3A at the end of lα3,4 and in the beginning of helix 4. These changes resulted in the designed protein, Cry3Bb.11035, that, unlike wild type Cry3Bb, forms Spontaneous channels with large conductances. Cry3Bb.11035 is also approximately three limes more active against SCRW larvae than WT Cry3Bb. Cry3Bb.11035 and its amino acid changes are listed in Table 10.
Cry3Bb.11032 was altered at residue 165 in helix α4, changing an asparate to glycine, as found in Cry3A. Cry3Bb.11032 is three-fold more active than WT Cry3Bb. The channel activity of Cry3Bb.11032 is much like Cry3Bb except when the designed protein is artificially incorporated into the membrane. A 16-fold increase in the initial channel conductances is observed compared to WT Cry3Bb (see Section 5.12.2). This increase in initial conductance presumably is due to enhanced quaternary structure, stability or higher-order structure.
In the WT Cry3Bb dimer structure, histidine, at position 231 in domain 1, makes hydrogen bond contacts with D288 (domain 1), Y230 (domain 1), and, through a network of water molecules, also makes contacts to D610 (domain 3), all of the opposite monomer. D610 and K235 (domain 1) also make contact. Replacing the histidine with an arginine, H231R, results, in one orientation, in the formation of a salt bridge to D610 of the neighboring monomer. In a second orientation, the contacts with D288 of the neighboring monomer, as appear in the WT structure, are retained. In either orientation, R231 does not hydrogen bond to Y230 of the opposite monomer but does make contact with K235 which retains is contacts to K610 (V. Cody, research communication). The shifting hydrogen bonds have changed the interactions between the different domains of the protein in the quaternary structure. Overall, fewer hydrogen bonds exist between domains 1 of the neighboring monomers and a much stronger bond has been formed between domains 1 and 3. Channel activity was found to be altered. Cry3Bb.11224 produces small, quickly gating channels like Cry3Bb. However, unlike WT Cry3Bb, Cry3Bb.11224 does not exhibit β-mercaptoethanol-dependent activation. Replacing H231 with arginine resulted in a designed Cry3Bb protein, Cry3Bb. 11224, exhibiting a 5-fold increase in bioactivity.
Cry3Bb.11226 is similar to Cry3Bb.11224, discussed in Section 4.8.5, in that the histidine at position 231 has been replacer. The amino acid change, H231T, results in the loss of β-mercaptoethanol dependent activation seen with WT Cry3Bb (see Section 5.12.1). The replacement of H231, a putative metal binding site, changes the interaction of regions in the quaternary structure resulting in a different type of channel activity. Cry3Bb.11226 is three-fold more active than WT Cry3Bb.
Cry3Bb.11221 has been re-designed in the lα3,4 region of Cry3Bb. The channels formed by Cry3Bb.1 1221 are much more well resolved than the conductances formed by WT Cry3Bb (see Section 5.12.6). Cry3Bb.11221 exhibits a 6.4-fold increase in bioactivity over that of WT Cry3Bb. The amino acid changes found in Cry3Bb.11221 are listed in Table 2.
The designed protein, Cry3Bb.11242, carrying the alteration R290V, forms small conductances immediately which grow rapidly and steadily to large conductances in about 3 min (see Section 5.12.7). This is contrast to WT Cry3Bb channels which take 30-45 min to appear and grow slowly over hours to large conductances. Cry3Bb.11242 also exhibits a 2.5-fold increase in bioactivity compared to WT Cry3Bb.
Cry3Bb.11230, unlike WT Cry3Bb, forms well resolved channels with long open states. These channels reach a maximum conductance of 3000 pS but do not continue to grow with time. Cry3Bb.11230 has been re-designed in the lβ1,α8 region of Cry3Bb and exhibits almost a 5-fold increase in activity against SCRW larvae (Table 9) and a 5.4-fold increase against WCRW larvae (Table 10) compared to WT Cry3Bb. The amino acid changes found in Cry3Bb.11230 are listed in Table 2.
Design Method 9: Design of Structural Residues
The specific three-dimensional structure of a protein is held in place by amino acids that may be buried or otherwise removed from the surface of the protein. These structural determinants can be identified by inspection of forces responsible for the surface structure positioning. The impact of these structural residues can then be enhanced to restrict molecular motion or diminished to enhance molecular flexibility.
Loops β2,3, β6,7 and β10,11, located in domain 2 of Cry3Bb, have been identified as important for bioactivity. The three loops are surface-exposed and structurally close together. Amino acid Q348 in WT structure, located in β-strand 2 just prior to lβ2,3, does not form any intramolecular contacts. However, replacing Q348 with arginine (Q348R) results in the formation of 2 new hydrogen-bonds between R348 and the backbone carbonyls of R487 and R488, both located in lβ10,11. The new hydrogen bonds may act to stabilize the structure formed by the three loops. Certainly, the structure around R348 is more tightly packed as determined by X-ray crystallography. The designed protein carrying this change, Cry3Bb.11095, is 4.6-fold more active than WT Cry3Bb.
Design Method 10: Combinatorial Analysis and Mutagenesis
Individual sites in the engineered Cry3Bb molecule can be used together to create a Cry3Bb molecule with activity even greater than the activity of any one site. This method has not been precisely applied to any δ-endotoxin. It is also not obvious that improvements in two sites can be pulled together to improve the biological activity of the protein. In fact, data demonstrates that improvements to 2 sites, when pulled together into a single construct, do not necessarily further improve the biological activity of Cry3Bb. In some cases, the combination resulted in decreased protein stability and/or activity. Examples of proteins with site combinations that resulted in improved activity compared to WT Cry3Bb but decreased activity compared to 1 or more of the "parental" proteins are Cry3Bb.11235, 11046, 11057 and 11058. Cry3Bb.11082, which contains designed regions from 4 parental proteins, retains the level of activity from the most active parental strain (Cry3Bb. 11230) but does not show an increase in activity. These proteins are listed in Table 7. The following are examples of instances where combined mutations have significantly improved biological activity.
Designed protein Cry3Bb.11231 contains the alterations found in Cry3Bb.11224 (H123R) and Cry3Bb.11228 (changes in lβ1,α8). The combination of amino acid changes found in Cry3Bb.11231 results in an increase in bioactivity against SCRW larvae of approximately 8-fold over that of WT Cry3Bb (Table 2). This increase is greater than exhibited by either Cry3Bb.11224 (5.0×) or Cry3Bb.11228 (4.1×) alone. Cry3Bb.11231 was also exhibits an 12.9-fold increase in activity compared to WT Cry3Bb against WCRW larvae (Table 10).
Designed Cry3Bb protein Cry3Bb.11081 was constructed by combining the changes found in Cry3Bb.11032 and Cry3Bb.11229 (with the exception of Y318C). Cry3Bb.11081 a 6.1 -fold increase in activity over WT Cry3Bb; a greater increase in activity than either of the individual parental proteins, Cry3Bb.11032 (3.1-fold) and Cry3Bb.11229 (2.5-fold).
Designed Cry3Bb protein Cry3Bb.11083 was constructed by combining the changes found in Cry3Bb.11036 and Cry3Bb.11095. Cry3Bb.11083 exhibits a 7.4-fold increase in activity against SCRW larvae compared to WT Cry3Bb; a greater increase than either Cry3Bb.11036 (4.3×) or Cry3Bb.11095 (4.6×). Cry3Bb.11083 also exhibits a 5.4-fold increase in activity against WCRW larvae compared to WT Cry3Bb (Table 10).
Designed Cry3Bb protein Cry3Bb.11084 was constructed by combining the changes found in Cry3Bb.11032 and the S311L change found in Cry3Bb.11228.
Cry3Bb.11084 exhibits a 7.2-fold increase in activity over that of WT Cry3Bb; a greater than either Cry3Bb.11032 (3×) or Cry3Bb.11228 (4×).
Designed Cry3Bb protein Cry3Bb.11098 was constructed to contain the following amino acid changes: D165G, H231R, S311L, N313T, and E317K. The nucleic acid sequence is given in SEQ ID NO:107, and the encoded amino acid sequence is given in SEQ ID NO:108.
Design Strategy 11: Alteration of Binding to Glycoproteins and to WCRW Brush Border Membranes
While the identity of receptor(s) for Cry3Bb is unknown, it is nonetheless important to increase the interaction of the toxin with its receptor. One way to improve the toxin-receptor interaction with knowing the identity of the receptor is to reduce or eliminate non-productive binding to other biomolecules. The inventors have observed that Cry3Bb binds non-specifically to bovine serum albumin (BSA) that has been glycosylated with a variety of sugar groups, but not to non-glycosylated BSA. Cry3A, which is not active on Diabrotica species, shows similar but even greater binding to glycosylated-BSA. Similarly, Cry3A shows greater binding to immobolized WCRW brush border membrane (BBM) than does WT Cry3Bb, suggesting that much of the observed binding is non-productive. It was reasoned that the non-specific binding to WCRW BBM occurs via glycosylated proteins, and that binding to both glycosylated-BSA and WCRW BBM is non-productive in reaction pathway to toxicity. Therefore reduction or elimination of that binding would lead to enhanced binding to the productive receptor and to enhanced toxicity. Potential binding sites for sugar groups were targeted for redesign to reduce the non-specific binding of Cry3Bb to glycoproteins and to immobilized WCRW BBM.
Cry3Bb-60, in which Cry3Bb has been cleaved at R159 in lα3,4, shows decreased binding to glycosylated-BSA and decreased binding to immobilized WCRW BBM. Cry3Bb-60 shows a 3.6-fold increase in bioactivity relative to WT Cry3Bb.
Cry3Bb.11221 has been redesigned in the lα3,4 region of domain 1, which is the region in which Cry3Bb is cleaved to produce Cry3Bb-60. Cry3Bb.11221 also shows decreased binding to both glycosylated-BSA and immobilized WCRW BBM, and exhibits a 6.4-fold increase in bioactivity over that of WT Cry3Bb. Together with data for Cry3Bb.60 (section 5.17.1) these data suggest that this loop region contributes substantially to non-productive binding of the toxin.
The lβ1,α8 region of Cry3Bb has been re-engineered to increase hydration (section 4.2.4) and enhance flexibility (section 4.4.3). Several proteins altered in this region, Cry3Bb.11228,11230, and 11237 demonstrate substantially lower levels of binding both glycosylated-BSA and immobilized WCRW BBM, and also show between 4.1- and 4.5-fold increases in bioactivity relative to WTF Cry3Bb.
The tendencies of Cry3Bb and some of its derivatives to bind to glycosylated-BSA and to WCRW BBM were determined using a BIAcore™ surface plasmon resonance biosensor. For glycosylated-BSA binding, the glycosylated protein was immobilized using standard NHS chemistry to a CM5 chip (BIAcore), and the solubilized toxin was injected over the glycosylated-BSA surface. To measure binding to WCRW BBM, brush border membrane vesicles (BBMV) purified from WCRW midguts (English et al., 1991) were immobilized on an HPA chip (BIAcore) then washed with either 10 mM KOH or with 40mM β-octylglucoside. The solubilized toxin was then injected over the resulting hybrid bilayer surface to detect binding. Protein concentration were determined by Protein Dye Reagent assay (BioRad) or BCA Protein Assay (Pierce).
Other methods may also be used to determine the same binding information. These include, but are not limited to, ligand blot experiments using labeled toxin, labeled glycosylated protein, or anti-toxin antibodies, affinity chrormatography, and in vitro binding of toxin to intact BBMV.
Construction of Plasmids with WT Cry3Bb Sequences
Standard recombinant DNA procedures were performed essentially as described by Sambrook et al., (1989).
pEG1701 (FIG. 11), contained in EG11204 and EG11037, was constructed by inserting the SphI-PstI fragment containing the cry3Bb gene and the cry1F terminator from pEG911 (Baum, 1994) into the SphI-PstI site of pEG854.9 (Baum et al., 1996), a high copy number B. thuringiensis--E. coli shuttle vector.
pEG1028 contains the HindIII fragment of cry3Bb from pEG1701 cloned into the multiple cloning site of pTZ18U at HindIII.
Construction of Plasmids with Altered Cry3Bb Genes
Plasmid DNA from E. coli was prepared by the alkaline lysis method (Maniatis et al., 1982) or by commercial plasmid preparation kits (examples: PERFECTprep™ kit, 5 Prime--3 Prime, Inc., Boulder CO; QIAGEN plasmid prep kit, QIAGEN Inc.). B thuringiensis plasmids were prepared from cultures grown in brain heart infusion plus 0.5% glycerol (BHIG) to mid logarithmic phase by the alkaline lysis method. When necessary for purification, DNA fragments were excised from an agarose gel following electrophoresis and recovered by glass milk using a Geneclean II® kit (BIO 101 Inc., La Jolla, Calif.). Alteration of the cry3Bb gene was accomplished using several techniques including site-directed mutagenesis, triplex PCR™, quasi-random PCR™ mutagenesis, DNA shuffling and standard recombinant techniques. These techniques are described in Sections 6.1, 6.2, 6.3, 6.4 and 6.5, respectively. The DNA sequences of primers used are listed in Section 7.
Site-Directed Mutagenesis
Site-directed mutagenesis was conducted by the protocols established by Kunkle (1985) and Kunkle et al. (1987) using the Muta-Gene™ M13 in vitro mutagenesis kit (Bio-Rad, Richmond, Calif.). Combinations of alterations to cry3Bb were accomplished by using the Muta-Gene Tm kit and multiple mutagenic, oligonucleotide primers.
pEG 1041, contained in EG11022, was constructed using the Muta-Gene™ kit, primer C, and single-stranded pEG1028 as the DNA template. The resulting altered cry3Bb DNA sequence was excised as a PflMI DNA fragment and used to replace the corresponding DNA fragment in pEG1701.
pEG1046, contained in EG11035, was constructed using the Muta-Gene™ kit, primer D, and single-stranded pEG1028 as the DNA template. The resulting altered cry3Bb DNA sequence was excised as a PflMI DNA fragment and used to replace the corresponding DNA fragment in pEG1701.
pEG1047, contained in EG11036, was constructed using the Muta-Gene™ kit, primer E, and single-stranded pEG1028 as the DNA template. The resulting altered cry3Bb DNA sequence was excised as a PflMI DNA fragment and used to replace the corresponding DNA fragment in pEG1701.
pEG1052, contained in EG11046, was constructed using the Muta-Gene™ kit, primers D and E, and single-stranded pEG1028 as the DNA template. The resulting altered cry3Bb DNA sequence was excised as a PflMI DNA fragment and used to replace the corresponding DNA fragment in pEG 1701.
pEG1054, contained in EG11048, was constructed using the Muta-Gene™ kit, primer F, and single-stranded pEG1028 as the DNA template. The resulting altered cry3Bb DNA sequence was excised as a PflMI DNA fragment and used to replace the corresponding DNA fragment in pEG1701.
pEG1057, contained in EG11051, was constructed using the Muta-Gene™ kit, primer G, and single-stranded pEG1028 as the DNA template. The resulting altered cry3Bb DNA sequence was excised as a PflMI DNA fragment and used to replace the corresponding DNA fragment in pEG1701.
Triplex PCR™
Triplex PCR™ is described by Michael (1994). This method makes use of a thermostable ligase to incorporate a phosphorylated mutagenic primer into an amplified DNA fragment during PCR™. PCR™ was preformed on a Perkin Elmer Cetus DNA Thermal Cycler (Perkin-Elmer, Norwalk, Conn.) using a AmpliTaq™ DNA polymerase kit (Perkin-Elmer) and SphI-linearized pEG1701 as the template DNA. PCR™ products were cleaned using commercial kits such as Wizard™ PCR™ Preps (Promega, Madison, Wis.) and QIAquick PCR™ Purification kit (QIAGEN Inc., Chatsworth, Calif.).
pEG1708 and pEG1709, contained in EG11222 and EG11223, respectively, were constructed by replacing the PflMI--PflMI fragment of cry3Bb in pEG1701 with PflMI-digested and gel purified PCR™ fragment altered at cry3Bb nucleotide positions 688-690, encoding amino acid Y230. Random mutations were introduced into the Y230 codon by triplex PCR™. Mutagenic primer MVT095 was phosphorylated and used together with outside primer pair FW001 and FW006. Primer MVT095 also contains a silent mutation at position 687, changing T to C, which, upon incorporation, introduces an additional EcoRI site into pEG1701.
Plasmids pEG1710, pEG1711 and pEG1712, contained in EG11224, EG11225 and EG11226, respectively, were created by replacing the PflMI--PflMI fragment of the cry3Bb gene in pEG1701 with PflMI-digested and gel purified PCR™ fragment altered at cry3Bb nucleotide positions 690-692, encoding H231. Random mutations were introduced into the H231 codon by triplex PCR™. Mutagenic primer MVT097 was phosphorylated and used together with outside primer pair FW001 and FW006. Primer MVT097 also contains a T to C sequence change at position 687 which, upon incorporation, results in an additional EcoRI site by silent mutation.
pEG1713 and pEG1727, contained in EG11227 and EG11242, respectively, were constructed by replacing the PflMI--PflMI fragment of the cry3Bb gene in pEG1701 with PflMI-digested and gel purified PCR™ fragment altered at cry3Bb nucleotide positions 868-870, encoding amino acid R290. Triplex PCR™ was used to introduce random changes into the R290 codon. The mutagenic primer, MVT091, was designed so that the nucleotide substitutions would result in approximately 36% of the sequences encoding amino acids D or E. MVT091 was phosphorylated and used together with outside primer pair FW001 and FW006.
Quasi-Random PCR™ Mutagenesis
Quasi-random mutagenesis combines the mutagenic PCR™ techniques described by Vallette et al. (1989), Tomic et al. (1990) and LaBean and Kauffman (1993). Mutagenic primers, sometimes over 70 nucleotides in length, were designed to introduce changes over nucleotide positions encoding for an entire structural region, such as a loop. Degenerate codons typically consisted of a ratio of 82% WT nucleotide plus 6% each of the other 3 nucleotides per position to semi-randomly introduce changes over the target region (LaBean and Kauffman, 1993). When possible, natural restriction sites were utilized; class 2s enzymes were used when natural sites were not convenient (Stemmer and Morris, 1992, list additional restriction enzymes useful to this technique). PCR™ was performed on a Perkin Elmer Cetus DNA Thermal Cycler (Perkin-Elmer, Norwalk, Conn.) using a AmpliTaq™ DNA polymerase kit (Perkin-Elmer) and SphI-linearized pEG1701 as the template DNA. Quasi-random PCR™ amplification was performed using the following conditions: denaturation at 94° C. for 1.5 min.; annealing at 50° C. for 2 min. and extension at 72° C. for 3 min., for 30cycles. The final 14 extension cycles were extended an additional 25 s per cycle. Primers concentration was 20 pM per reaction or 40 μM for long, mutagenic primers. PCR™ products were cleaned using commercial kits such as Wizard™ PCR™ Preps (Promega, Madison, Wis.) and QIAquickPCR™ Purification kit (QIAGEN Inc., Chatsworth, Calif). In some instances PCR™ products were treated with Klenow Fragment (Promega) following the manufacturer's instructions to fill in any single base overhangs prior to restriction digestion.
EG1707, contained in EG11221, was constructed by replacing the PflMI--PflMI fragment of the cry3Bb gene in pEG1701 with PflMI-digested and gel purified PCR™ fragment altered at cry3Bb nucleotide positions 460-480, encoding lα3,4 amino acids 154-160. Primer MVT075, which includes a recognition site for the class 2s restriction enzyme BsaI, and primer FW006 were used to introduce changes into this region by quasi-random mutagenesis. Primers MVT076, also containing a BsaI site, and primer FW001 were used to PCR™ amplify a "linker" fragment. Following PCR™ amplification, both products were cleaned, end-filled, digested with BsaI and ligated to each other. Ligated fragment was gel purified and used as template for PCR™ amplification using primer pair FW001 and FW006. PCR™ product was cleaned, digested with PflMI, gel purified and ligated into PflMI-digested and purified pEG1701 vector DNA.
pEG1720 and pEG1726, contained in EG11234 and EG11241, respectively, were constructed by replacing the PflMI--PflMI fragment of the cry3Bb gene in pEG1701 with PflMI-digested and gel purified PCR™ fragment altered at cry3Bb nucleotide positions 859-885, encoding lα7,β1 amino acids 287-295. Quasi-random PCR™ mutagenesis was used to introduce changes into this region. Mutagenic primer MVT111, designed with a BsaI site, and primer FW006 were used to introduce the changes. Primer pair MVT094, also containing a BsaI site, and FW001 were used to amplify the linker fragment. The PCR™ products were digested with BsaI, gel purified then ligated to each other. Ligated product was PCR™ amplified using primer pair FW001 and FW006, digested with PflMI.
pEG1714, pEG1715, pEG1716, pEG1718, pEG1719, pEG1722, pEG1723, pEG1724 and pEG1725, contained in EG11228, EG11229, EG11230, EG11232, EG11233, EG11236, EG11237, EG11238 and EG11239, respectively, were constructed by replacing the PflMI--PflMI fragment of the cry3Bb gene in pEG1701 with PflMI-digested and gel purified PCR™ fragment altered at cry3Bb nucleotide positions 931-954, encoding lβ1,α8 amino acids 311-318. Quasi-random PCR™ mutagenesis was used to introduce changes into this region using mutagenic primer MVT103 and primer FW006. Primers FW001 and FW006 were used to amplify a linker fragment. The PCR™ products were end-filled using Klenow and digested with BamHI. The larger fragment from the FW001-FW006 digest was gel purified then ligated to the digested MVT103-FW006 fragment. Ligated product was gel purified and amplified by PCR™ using primer pair FW001 and FW006. The amplified product was digested with PflMI and gel purified prior to ligation into PflMI-digested and purified pEG1701 vector DNA.
Plasmids carrying alterations of cry3Bb WT sequence at nucleotides 1051-1065, encoding structural region lβ2,3 of Cry3Bb, were constructed by replacing the MluI-SpeI fragment of pEG1701 with isolated MluI- and SpeI-digested PCR™ product. The PCR™ product was generated by quasi-random PCR™ mutagenesis were mutagenic primer MVT081 was paired with FW006. These plasmids as a group are designated pEG1701.lβ2,3.
Plasmids containing mutations of the cry3Bb WT sequence at nucleotides 1234-1248, encoding structural region lβ6,7 of Cry3Bb, were constructed by replacing the MluI-SpeI fragment of pEG1701 with isolated MluI- and SpeI-digested PCR™ product. The PCR™ product was generated by quasi-random PCR™ mutagenesis where mutagenic primer MVT085 was paired with primer WD115. Primer pair MVT089 and WD112 were used to amplify a linker fragment. Both PCR™ products were digested with TaqI and ligated to each other. The ligation product was gel purified and PCR™ amplified using primer pair MVT089 and FW006. The amplified product was digested with MluI and SpeI and ligated into MluI and SpeI digested and purified pEG1701 vector DNA. These plasmids as a group are designated pEG1701.lβ6,7.
Plasmids containing mutated cry3Bb sequences at nucleotides 1450-1467, encoding structural region lβ10,11 of Cry3Bb, were constructed by replacing the SpeI-PstI fragment of pEG1701 with isolated SpeI- and PstI-digested PCR™ product. The PCR™ product was generated by quasi-random PCR™ mutagenesis where mutagenic primer MVT105 was paired with primer MVT070. Primer pair MVT092 and MVT083 were used to generate a linker fragment. (MVT083 is a mutagenic oligo designed for another region. The sequence changes introduced by MVT083 are removed following restriction digestion and do not impact the alteration of cry3Bb in the lβ10,11 region.) Both PCR™ products were digested with BsaI, ligated together, and the ligation product PCR™ amplified with primer pair MVT083 and MVT070. The resulting PCR™ product was digested with speI and PstI, and gel purified. These plasmids as a group are designated pEG1701.lβ10,11.
DNA Shuffling
DNA-shuffling, as described by Stemmer (1994), was used to combine individual alterations in the cry3Bb gene.
pEG1084, pEG1085, pEG1086, and pEG1087, contained in EG11081, EG11082, EG11083, and EG11084, respectively, were recovered from DNA-shuffling. Briefly, PflMI DNA fragments were generated using primer set A and B and each of the plasmids pEG1707, pEG1714, pEG1715, pEG1716, pEG1041, pEG1046, pEG1047, and pEG1054 as DNA templates. The resulting DNA fragments were pooled in equal-molar amounts and digested with DNaseI and 50-100 bp DNA fragments were recovered from an agarose gel by three successive freeze-thaw cycles: three min in a dry-ice ethanol bath followed by complete thawing at 50° C. The recovered DNA fragments were assembled by primerless-PCR™ and PCR™-amplified using the primer set A and B as described by Stemmer (1994). The final PCR™-amplified DNA fragments were cut with PflMI and used to replace the corresponding cry3Bb PflMI DNA fragment in pEG1701.
Recombinant DNA Techniques
Standard recombinant DNA procedures were performed essentially as described by Sambrook et al. (1989).
pEG1717, contained in EG11231, was constructed by replacing the small BglII fragment of pEG1710 with the small BglII fragment from pEG1714.
pEG1721, contained in EG11235, was constructed by replacing the small BglII fragment from pEG1710 with the small BglII fragment from pEG1087.
pEG1062, contained in EG11057, was constructed by replacing the NcoI DNA fragment containing ori 43 from pEG1054 with the isolated NcoI DNA fragment containing ori 43 and the alterations in cry3Bb from pEG 1046.
pEG1063, contained in EG11058, was constructed by replacing the NcoI DNA fragment containing ori 43 from pEG1054 with the isolated Ncol DNA fragment containing ori 43 and the alterations in cry3Bb from pEG 1707.
pEG1095, contained in EG11095, was constructed by replacing the MluI-SpeI DNA fragment in pEG1701 with the corresponding MluI-SpeI DNA fragment from pEG1086.
Primers Utilized in Constructing Cry3Bb* Variants
Shown below are the primers used for site-directed mutagenesis, triplex PCR™ and quasi-random PCR™ to prepare the cry3Bb* variants as described above. Primers were obtained from Ransom Hill Bioscience, Inc. (Ramona, Calif.) and Integrated DNA Technologies, Inc. (Coralville, Iowa). The specific composition of the primers containing particular degeneracies at one or more residues is given in Section 5.30, Example 30.
5'-AGACAACTCTACAGTAAAAGATG-3'
5'-GGTAATTGGTCAATAGAATC-3'
5'-CAGAAGATGTTGCTGAATTCNNNCATAGACAATTAAAAC-3'
5'-GATGTTGCTGAATTCTATNNNAGACAATTAAAAC-3'
5'-CCCATTTTATGATATTBDNTTATACTCAAAAGG-3'
5'-AGCTATGCTGGTCTCGGAAGAAAEFNFFNFJNJFJFJNFINJFJAAAAGAAGCCAAGATCGAAT-3'
5'-GGTCACCTAGGTCTCTCTTCCAGGAATTTAACGCATTAAC-3'
5'-AGCTATGCTGGTCCCATTTJEHIEJEJJEIIKRRJEHEIJEENIIIGTTAAAACAGAACTAAC-3'
5'-ATCCAGTGGGGTCTCAAATGGGAAAAGTACAATTAG-3'
5'-CATTTTTACGGATCCAATTTTTJFFFJNEEJEFNFJNFEILEIJEOGGACCAACTTTTTTGAG-3'
5'-GAAITTTCATACGCGTCTTCAACCGGJEHJJJINMEEIEJTCTTTCAATTATTGGTCTGG-3'
5'-AAAAGTTTATCGAACTATAGCTAATACAGACGTAGCGGCTJQQFFNEEJIIJEEIGTATATTTAGGTGTTACG-3'
5'-GGAGTTCCATTTGCTGGGGC-3'
5'-ATCTCCATAAAATGGGG-3'
5'-GCGAAGTAAAAGAAGCCAAGGTCGAATAAGGG-3'
5'-CCTTTAAGTTTGCGAAATCCACACAGCCAAGGTCGAATAAGGG-3'
5'-CCCATTTTATGATGTTCGGTTATACCCAAAAGGGG-3'
5'-GGCCAAGTGAAGACCCATGGAAGGC-3'
5'-GCAGTTTCCGGATTCGAAGTGC-3'
5'-CCGCTACGTCTGTATTA-3'
5'-AGCTATGCTGGTCTCTTCTTAEJIFEIIEFFIJFIJIINACAATTCCATTTTTTACTTGG-3'
5'-ATCCAGTTFGGGTCTCTAAGAAACAAACCGCGTAATTAAGC-3'
5'-CCTCAAGGGTTATAACATCC-3'
5'-GTACAAAAGCTAAGCTTTIEJIINPEEMEEIJNJESCGAACTATAGCTAATACAG-3'
Sequence Analysis of Altered Cry3Bb Genes
E. coli DH5α™ (GIBCO BRL, Gaithersburg, Md.), JM110 and Sure™ (Stratagene, La Jolla, Calif.) cells were sometimes used amplify plasmid DNA for sequencing. Plasmids were transformed into these cells using the manufacturers' procedures. DNA was sequenced using the Sequenase® 2.0 DNA sequencing kit purchased from U.S. Biochemical Corporation (Cleveland, Ohio). The plasmids described in Section 6, their respective divergence from WT cry3Bb sequence, the resulting amino acid changes and the protein structure site of the changes are listed in Table 11.
TABLE 11
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DNA SEQUENCE CHANGES OF CRY3BB* GENES
AND RESULTING AMINO ACID SUBSTITUTIONS OF THE CRY3BB* PROTEINS
Structural Site
Plasmid
cry3Bb* DNA Sequence Cry3Bb* Amino Acid Sequence
of Alteration
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pEG1707
A460T, C461T, A462T, C464A, T465C, T466C, T467A,
T154F, P155H, L156H, L158R
1α3,4
A468T, A469T, G470C, T472C, T473G, G474T,
A477T, A478T, G479C
pEG1708
T687C, T688C, A689T, C691A, A692G
Y230L, H231S α6
pEG1709
T667C, T687C, T688A, A689G, C691A, A692G
S223P, Y230S α6
pEG1710
T687C, A692G H231R α6
pEG1711
T687C, C691A H231N, T241S α6
pEG1712
T687C, C691A, A692C, T693C
H231T α6
pEG1713
C868A, G869A, G870T R290N 1α7,β1
pEG1714
C932T, A938C, T942G, G949A, T954C
S311L, N313T, E317K
1β1,α8
pEG1715
T931A, A933C, T942A, T945A, G949A, A953G,
S311T, E317K, Y318C
1β1,α8
T954C
PEG1716
T931G, A933C, C934G, T945G, C946T, A947G,
S311A, L312V, Q316W
1β1,α8
G951A, T954C
pEG1717
T687C, A692G, C932T, A938C, T942G, G949A,
H231R, S311L, N313T, E317K
α6, 1β1,α8
T954C
pEG1718
T931A, A933G, T935C, T936A, A938C, T939C,
S311T, L312P, N313T, E317N
1β1,α8
T942C, T945A, G951T, T954C
pEG1719
T931G, A933C, T936G, T942C, C943T, T945A,
S311A, Q316D 1β1,α8
C946G, G948C, T954C
pEG1720
T861C, T866C, C868A, T871C, T872G, A875T,
I289T, L291R, Y292F, S293R
1α7,β1
T877A, C878G, A882G
pEG1721
T687C, A692G, C932T H231R, S311L α6, 1β1, α8
pEG1722
T931A, C932T, A933C, T936C, T942G, T945A, T954C
S311I 1β1,α8
pEG1723
T931A, C932T, A933C, T936C, A937G, A938T,
S311I, N313H 1β1,α8
C941A, T942C, T945A, C946A, A947T, A950T,
T954C
pEG1724
A933C, T936C, A937G, A938T, C941A, T942C,
N313V, T314N, Q316M, E317V
1β1,α8
T945A, C946A, A947T, A950T, T954C
pEG1725
A933T, A938G, T939G, T942A, T944C, T945A,
N313R, L315P, Q316L, E317A
1β1,α8
A947T, G948T, A950C, T954C
pEG1726
A860T, T861C, G862A, C868T, G869T, T871C,
Y287F, D288N, R290L
1α7,β1
A873T, T877A, C878G, A879T
pEG1727
C868G, G869T R290V 1α7,β1
pEG1041
A494G D165G α4
pEG1046
G479A, A481C, A482C, A484C, G485A,
S160N, K161P, P162H, D165G
α4
A486C, A494G
pEG1047
A865G, T877C I289V, S293P 1α7,β1
pEG1052
G479A, A481C, A482C, A484C, G485A, A486C,
S160N, K161P, P162H, D165G,
α4, 1α7,β1
A494G, A865G, T877C I289V, S293P
pEG1054
T309A, Δ310, Δ311, Δ312
D103E, ΔA104
1α2a,2b
pEG1057
A565G, A566G K189G 1α4,5
pEG1062
T309A, Δ310, Δ311, Δ312, G479A, A481C,
D103E, ΔA104, S160N,
1α2a,2b α4
A484C, G485A, A486C, A494G
P162H, D165G
pEG1063
T309A, Δ310, Δ311, Δ312, A460T, C461T,
D103E, ΔA104, T154F,
1α2a,2b 1α3,4
C464A, T465C, T466C, T467A, A468T, A469T,
L156H, L158R
G470C, T472C, T473G, G474T, A477T, A478T,
G479C
pEG1084
A494G, T931A, A933C, T942A, T945A, G949A,
D165G, S311T, E317K
α4, 1β1,α8
T954C
pEG1085
A494G, A865G, T877C, T914C, T931G, A933C,
D165G, 1289V, S293P, F305S,
α4, 1α7,β1
β1, 1β1,α8
C934G, T945G, C946T, A947G, G951A, T954C,
S311A, L312V, Q316W, Q348R,
β2, β3b
A1043G, T1094C V365A
pEG1086
A865G, T877C, A1043G 1289V, S293P, Q348R
1α7,β1, β2
pEG1087
A494G, C932T D165G, S311L α4, 1β1,α8
pEG1095
A1043G Q348R β2
__________________________________________________________________________
Expression of Cry3Bb* Proteins
LB agar was prepared using a standard formula (Maniatis et al., 1982). Starch agar was obtained from Difco Laboratories (Detroit, Mich.) and supplemented with an additional 5 g/l of agar. C2 liquid medium is described by Donovan et al. (1988). C2 medium was sometimes prepared without the phosphate buffer (C2-P). All cultures were incubated at 25° C. to 30° C.; liquid cultures were also shaken at 250 rpm, until sporulation and lysis had occurred.
pEG1701 and derivatives thereof were introduced into acrystalliferious B. thuringiensis var. kurstaki EG7566 (Baum, 1994) or EG10368 (U.S. Pat. No. 5,322,687) by the electroporation method of Macaluso and Mettus (1991). In some cases, the method was modified as follows to maximize the number of transformants. The recipient B. thuringiensis strain was inoculated from overnight growth at 30° C. on LB agar into brain heart infusion plus 0.5% glycerol, grown to an optical density of approximately 0.5 at 600 nm, chilled on ice for 10 min, washed 2× with EB and resuspended in a 1/50 volume of EB. Transformed cells were selected on LB agar or starch agar plus 5 μg/ml chloramphenicol. Visual screening of colonies was used to identify transformants producing crystalline protein; those colonies were generally more opaque than colonies that did not produce crystalline protein.
A transformant containing an altered cry3Bb* gene encoding an altered Cry3Bb* protein is designated by an "EG" number, e.g., EG11231. The altered Cry3Bb* protein is designated Cry3Bb followed by the strain number, e.g., Cry3Bb.11231. Collections of proteins with alterations at a structural site are designated Cry3Bb followed by the structural site, e.g., Cry3Bb.lβ2,3. Table 12 lists the plasmids pertinent to this invention, the new B. thuringiensis strains containing the plasmids, the acrystalliferous B. thuringiensis recipient strain used, and the proteins produced by the new strains.
Generation and Characterization of Cry3Bb-60
Cry3Bb-producing strain EG7231 (U.S. Pat. No. 5,187,091) was grown in C2 medium plus 3 mg/ml chloramphenicol. Following sporulation and lysis, the culture was washed with water and Cry3Bb protein purified by the NaBr solubilization and recrystallization method of Cody et at. (1992). Protein concentration was determined by BCA Protein Assay (Pierce, Rockford, Ill.). Recrystallized protein was solubilized in 10 ml of 50 mM KOH per 100 mg of Cry3Bb protein and buffered to pH 9.0 with 100 mM CAPS (3-[cyclohexylamino]-1-propanesulfonic acid), pH 9.0. The soluble toxin was treated with trypsin at a weight ratio of 50 mg toxin to 1 mg trypsin for 20 min to overnight at room temperature. Trypsin cleaves proteins on the carboxyl side of available arginine and lysine residues. For 8-dose bioassay, the solubilization conditions were altered slightly to increase the concentration of protein: 50 mM KOH was added dropwise to 2.7 ml of a 12.77 mg/ml suspension of purified Cry3Bb* until crystal solubilization occurred. The volume was then adjusted to 7 ml with 100 mM CAPS, pH 9.0.
TABLE 12
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PLASMIDS CARRYING ALTERED CRY3BB* GENES
TRANSFORMED INTO B. THURINGIENSIS
FOR EXPRESSION OF ALTERED CRY3BB* PROTEINS
Plasmid Designation
New BT Strain Expressed Protein
______________________________________
pEG1701 EG11204 WT Cry3Bb
pBG1701 EG11037 WT Cry3Bb
pEG1707 EG11221 Cry3Bb.11221
pBG1708 BG11222 Cry3Bb.11222
pEG1709 EG11223 Cry3Bb.11223
pEG1710 EG11224 Cry3Bb.11224
pEG1711 EG11225 Cry3Bb.11225
pEG1712 EG11226 Cry3Bb.11226
pEG1713 EG11227 Cry3Bb.11227
pEG1714 EGI1228 Cry3Bb.11228
pEG1715 EG11229 Cry3Bb.11229
pEG1716 EG11230 Cry3Bb.11230
pEG1717 EG11231 Cry3Bb.11231
pEG1718 EG11232 Cry3Bb.11232
pEG1719 EG11233 Cry3Bb.11233
pEG1720 EG11234 Cry3Bb.11234
pEG1721 EG11235 Cry3Bb.11235
pEG1722 EG11236 Cry3Bb.11236
pEG1723 EG11237 Cry3Bb.11237
pEG1724 EG11238 Cry3Bb.11238
pEG1725 EG11239 Cry3Bb.11239
pEG1726 EG11241 Cry3Bb.11241
pEG1727 EG11242 Cry3Bb.11242
pEG1041 EG11032 Cry3Bb.11032
pEG1046 EG11035 Cry3Bb.11035
pEG1047 EG11036 Cry3Bb.11036
pEG1052 EG11046 Cry3Bb.11046
pEG1054 EG11048 Cry3Bb.11048
pEG1057 EG11051 Cry3Bb.11051
pEG1062 EG11057 Cry3Bb.11057
pEG1063 EG11058 Cry3Bb.11058
pEG1084 EG11081 Cry3Bb.11081
pEG1085 EG11082 Cry3Bb.11082
pEG1086 EG11083 Cry3Bb.11083
pEG1087 EG11084 Cry3Bb.11084
pEG1095 EG11095 Cry3Bb.11095
pEG1098 EG11098 Cry3Bb.11098
pEG1701.1β2,3
collection of unnamed strains
Cry3Bb.1β2,3
pEG1701.1β6,7
collection of unnamed strains
Cry3Bb.1β6,7
pEG1701.1β10,11
collection of unnamed strains
Cry3Bb.1β10,11
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The molecular weight of the predominant trypsin digestion fragment of Cry3Bb was determined to be 60 kDa by SDS-polyacrylamide gel electrophoresis (SDS-PAGE) analysis using commercial molecular weight markers. This digestion fragment is designated Cry3Bb-60. No further digestion of the 60 kDa cleavage product was observed.
To determine the NH2 -terminal sequence of Cry3Bb-60, the trypsin digest was fractionated by SDS-PAGE and transferred to Immobilon TMP membrane (Millipore Corporation, Bedford, Mass.) following standard western blotting procedures. After transfer, the membrane was rinsed twice with water then stained with 0.025% Coomassie Brilliant Blue R-250 plus 40% methanol for 5 min, destained with 50% methanol and rinsed in water. The Cry3Bb.60 band was excised with a razor blade. NH2 -terminal sequencing was performed at the Tufts Medical School, Department of Physiology (Boston, Mass.) using standard automated Edman degradation procedures. The NH2 -terminal amino acid sequence was determined to be SKRSQDR (SEQ ID NO:96), corresponding to amino acids 160-166 of Cry3Bb. Trypsin digestion occurred on the carboxyl side of amino acid R159 resulting in the removal of helices 1-3.
Bioactivity of Cry3Bb* Proteins
Cultures for 1-dose bioassays were grown in C2-P plus 5 μg/ml chloramphenicol (C2-P/cm5) then diluted with 3 volumes of 0.005% Triton X-100®. The protein concentrations of these cultures were not determined. Cultures for 8-dose bioassays were grown in C2/cm5, washed 1-2 times with 1-2 volumes of sterile water and resuspended in 1/10 volume of sterile 0.005% Triton X-100®. The toxin protein concentration of each concentrate was determined as described by Brussock and Currier (1990), omitting the treatment with 3 M HEPES. The protein concentration was adjusted to 3.2 mg/ml in 0.005% Triton X-100® for the top dose of the assay. Cry3Bb.60 was produced and quantified for 8-dose assay as described in Section 9.1.
Diabrotica undecimpunctata howardi Barber (southern corn rootworm or SCRW) and Diabrotica virgifera virgifiera LeConte (western corn rootworm or WCRW) larvae were reared as described by Slaney et al. (1992). Eight-dose assays and probit analyses were performed as described by Slaney et al. (1992). Thirty-two larvae were tested per dose at 50 μl of sample per well of diet (surface area of 175 mm2). Positive controls were WT Cry3Bb-producing strains EG11037 or EG11204. All bioassays were performed using 128-well trays containing approximately 1 ml of diet per well with perforated mylar sheet covers (C-D International Inc., Pitman, N.J.). One-dose assays were performed essentially the same except only 1 dose was tested per strain. All assay were replicated at least twice.
Results from 1-dose assays are expressed as the relative mortality (RM) of the experimental strain compared to WT (% mortality of experimental culture divided by % mortality of WT culture). Altered and improved Cry3Bb proteins derived from plasmids constructed using PCR™ methods introducing random or semi-random changes into the cry3Bb gene sequence were distinguished from other altered but not improved Cry3Bb proteins by replicated, 1-dose assay against SCRW larvae. Those proteins showing increased activity (defined as RM≧1.5) compared to WT Cry3Bb or, in the case of proteins with combinations of altered sites, compared to a "parental" altered Cry3Bb protein were further characterized by 8-dose assay. The overall RM "pattern" produced by 1-dose assay results from a collection of proteins carrying random or semi-random alterations within a single structural region, e.g., in lβ2,3, can be used to determine if that structural region is important for bioactivity. Retention of WT levels of activity (RM≈1) indicate changes are tolerated in that region. Overall loss of activity (RM<1) distinguishes the region as important for bioactivity.
Cry3Bb.lβ2.3 protein are a collection of proteins altered in the lβ2,3 region of Cry3Bb (see Section 5.3.4). Typical results of 1-dose assays of these altered proteins are shown in FIG. 12. The RM values for Cry3Bb.lβ2,3 proteins are less than 1, with a few exceptions of values close to 1, indicating that this region is important for toxicity.
Cry3Bb.lβ6,7 proteins are a collection of proteins altered in the lβ6,7 region of Cry3Bb (see Section 5.3.5). Typical results of 1-dose assays of these altered proteins are shown in FIG. 13. With a few exceptions of values close to 1, the RM values for Cry3Bb.lβ6,7 proteins are less than 1, indicating that this region is important for toxicity.
Cry3Bb.lβ10,11 proteins are a collection of proteins altered in the lβ10,11 region of Cry3Bb (see Section 5.3.6). Typical results of 1-dose assays of these altered proteins are shown in FIG. 14. With a few exceptions of values close to 1, the RM values for Cry3Bb.lβ10,11 proteins are less than 1, indicating that this region is important for bioactivity.
Results from 8-dose assays are expressed as an LC50 value (protein concentration giving 50% mortality) with 95% confidence intervals. The LC50 values with 95% confidence intervals of altered Cry3Bb proteins showing improved activities against SCRW larvae and LC50 values of the WT Cry3Bb control determined at the same time are listed in Table 13 along with the fold increase over WT activity for each improved protein.
TABLE 13
______________________________________
DESIGNED CRY3BB PROTEINS WERE TESTED AGAINST
SCRW LARVAE IN REPLICATED, 8-DOSE ASSAYS
TO DETERMINE THE LC.sub.50 VALUES
LC.sub.50 μg/well (95% C.I.)
Fold
Improved WT Cry3Bb Increase Over
Protein Improved Protein
Control WT Activity
______________________________________
Cry3Bb.60
6.7 (5.3-8.4) 24.1 (15-39)
3.6×
Cry3Bb.11221
3.2 (2.5-4) 20.5 (14.5-29)
6.4×
Cry3Bb.11222
7.3 (6-9) 29.4 (23-37)
4.0×
Cry3Bb.11223
10.5 (9-12) 29.4 (23-37)
2.8×
Cry3Bb.11224
6.5 (5.1-8.2) 32.5 (25-43)
5.0×
Cry3Bb.11225
13.7 (11-16.8) 49.5 (39-65)
3.6×
Cry3Bb.11226
16.7 (10.6-24.2)
49.5 (39-65)
3.0×
Cry3Bb.11227
11.1 (9.1-13.5)
21.3 (16-28)
1.9×
Cry3Bb.11228
8.0 (6.6-9.8) 32.9 (25-45)
4.1×
Cry3Bb.11229
7.2 (5.8-8.8) 18.2 (15-22)
2.5×
Cry3Bb.11230
7.0 (5.8-8.6) 32.9 (25-45)
4.7×
Cry3Bb.11231
3.3 (3.0-3.7) 26.1 (22-31)
7.9×
Cry3Bb.11232
6.4 (5.4-7.7) 32.9 (25-45)
5.1×
Cry3Bb.11233
15.7 (12-20) 32.9 (25-45)
2.2×
Cry3Bb.11234
7 (6-9) 29 (22-39)
4.1×
Cry3Bb.11235
4.2 (3.6-4.9) 13.3 (10-17)
3.2×
Cry3Bb.11236
11.6 (9-15) 36.4 (27-49)
3.1×
Cry3Bb.11237
6.8 (4-11) 36.4 (27-49)
5.4×
Cry3Bb.11238
13.9 (11-17) 36.4 (27-49)
2.6×
Cry3Bb.11239
13.0 (10-16) 36.4 (27-49)
2.8×
Cry3Bb.11241
11 (7-16) 29 (22-39)
2.6×
Cry3Bb.11242
11.9 (9.2-16) 30 (23-38)
2.5×
Cry3Bb.11032
4.2 (3.6-4.9) 13.3 (10-17)
3.1×
Cry3Bb.11035
10.3 (8-13) 27.9 (23-34)
2.7×
Cry3Bb.11036
6.5 (5.1-7.9) 27.9 (23-34)
4.3×
Cry3Bb.11046
12.1 (8-19) 31.2 (25-39)
2.6×
Cry3Bb.11048
8.3 (6-11) 35.4 (24-53)
4.3×
Cry3Bb.11051
11.8 (8-16) 35.4 (24-53)
3.0×
Cry3Bb.11057
8.8 (7-11) 29.5 (24-36)
3.4×
Cry3Bb.11058
9.6 (6-14) 33.4 (27-43)
3.5×
Cry3Bb.11081
8.5 (7-11) 51.5 (37-79)
6.1×
Cry3Bb.11082
10.6 (8-13) 51.5 (37-79)
4.9×
Cry3Bb.11083
7.0 (5-10) 51.5 (37-79)
7.4×
Cry3Bb.11084
7.2 (4-12) 51.5 (37-79)
7.2×
Cry3Bb.11095
11.1 (9-14) 51.5 (37-79)
4.6×
Cry3Bb.11098
______________________________________
WCRW larvae are delicate and difficult to work with. Therefore, only some of the designed Cry3Bb showing improved activity against SCRW larvae were also tested against WCRW larvae in 8-dose assays. The LC50 determinations for the designed Cry3Bb proteins are shown in Table 14 along with the LC50 values of the WT Cry3Bb control determined at the same time.
TABLE 14
______________________________________
CRY3BB* PROTEINS SHOWING IMPROVED ACTIVITY
AGAINST SCRW LARVAE ALSO SHOW
IMPROVED ACTIVITY AGAINST WCRW LARVAE
LC.sub.50 μg/well (95% C.I.)
Fold
Improved WT Cry3Bb Increase Over
Protein Improved Protein
Control WT Activity
______________________________________
EG11083 6.3 (4.7-8.2) 63.5 (46-91)
10.1×
EG11230 4.5 (2.1-7.4) 24.2 (13-40)
5.4×
EG11231 2.5 (1.7-3.6) 32.2 (14-67)
12.9×
______________________________________
Channel Activity
Ion channels produced by Cry3Bb and some of its derivatives were measured by the methods described by Slatin et al. (1990). In some instances, lipid bilayers were prepared from a mixture of 4:1 phophatidylethanolamine (PE): phosphatidylcholine (PC). Toxin protein was solubilized from washed, C2 medium, B. thuringiensis cultures with 12 mM KOH. Following centrifugation to remove spores and other debris, 10 μg of soluble toxin protein was added to the cis compartment (4.5 ml volume) of the membrane chamber. Protein concentration was determined using the BCA Protein Assay (Pierce)
Upon exposure to black lipid membranes, Cry3Bb forms ion channels with various conductance states. The channels formed by Cry3Bb are rarely discrete channels with well resolved open and closed states and usually require incubation of the toxin with the membrane for 30-45 min before any channel-like events are observed. After formation of the initial conductances, the size increases from approximately 200 pS to over 10,000 pS over 2-3 h. Only the small conductances (≦200 pS) are voltage dependent. Over 200 pS, the conductances are completely symmetric. Cry3Bb channels also exhibit β-mercaptoethanol-dependent activation, growing from small channel conductances of ˜200 pS to several thousand pS within 2 min of the addition of β-mercaptoethanol to the cis compartment of the membrane chamber.
The channel activity of Cry3Bb.11032 is much like WT Cry3Bb when the solubilized toxin protein is added to the cis compartment of the membrane chamber. However, when this protein is artificially incorporated into the membrane by forming or "painting" the membrane in the presence of the Cry3Bb.11032 protein, a 16-fold increase in the initial channel conductances is observed (˜4000 pS). This phenomenon is not observed with WT Cry3 Bb.
Upon exposure to artificial membranes, the Cry3Bb.11035 protein spontaneously forms channels that grow to large conductances within a relatively short time span (˜5 min). Conductance values ranges from 3000-6000 pS and, like WT Cry3Bb, are voltage dependent at low conductance values.
The Cry3Bb.11048 protein is quite different than WT Cry3Bb in that it appears not to form channels at all, but, rather, forms symmetrical pores with respect to voltage. Once the pore is formed, it remains open and allows a steady conductance ranging from 25 to 130 pS.
The metal binding site of WT Cry3Bb formed by H231 in the dimer structure was removed in proteins Cry3Bb.11224 and Cry3Bb.11226. The conductances formed by both designed proteins are identical to that of WT Cry3Bb with the exception that neither of the designed proteins exhibits β-mercaptoethanol-dependent activation.
Cry3Bb. 11221 protein has been observed to immediately form small channels of 100-200 pS with limited voltage dependence. Some higher conductances were observed at the negative potential. In other studies the onset of activity was delayed by 27 min, which is more typical for WT Cry3Bb. Unlike WT Cry3Bb, however, Cry3Bb.11221 forms well resolved, 600 pS channels with long open states. The protein eventually reaches conductances of 7000 pS.
Cry3Bb.11242 protein forms small conductances immediately upon exposure to an artificial membrane. The conductances grow steadily and rapidly to 6000 pS in approximately 3 min. Some voltage dependence was noted with a preference for a negative imposed voltage.
Unlike WT Cry3Bb, Cry3Bb.11230 forms well resolved channels with long open states that do not continue to grow in conductance with time. The maximum observed channel conductances reached 3000 pS. FIG. 15 illustrates the difference between the channels formed by Cry3Bb and Cry3Bb.11230.
Cry3Bb.60 forms well resolved ion channels within 20 min of exposure to an artificial membrane. These channels grow in conductance and frequency with time. The behavior of Cry3Bb.60 in a planar lipid bilayer differs from Cry3Bb in two significant ways. The conductances created by Cry3Bb.60 form more quickly than Cry3Bb and, unlike Cry3Bb, the conductances are stable, having well resolved open and closed states definitive of stable ion channels (FIG. 16).
Primer Compositions
TABLE 15 ______________________________________ SEQ ID NO: 83 % of Nucleotide in mixture CodeA T G C ______________________________________ N 25 25 25 25 ______________________________________
TABLE 16 ______________________________________ SEQ ID NO: 84 % of Nucleotide in mixture CodeA T G C ______________________________________ N 25 25 25 25 ______________________________________
TABLE 17 ______________________________________ SEQ ID NO: 85 % of Nucleotide in mixture CodeA T G C ______________________________________ B 16 16 52 16D 70 10 10 10N 25 25 25 25 ______________________________________
TABLE 18 ______________________________________ SEQ ID NO: 86 % of Nucleotide in mixture Code A T G C ______________________________________ E 82 6 6 6F 6 6 6 82J 6 82 6 6 I 6 6 82 6N 25 25 25 25 ______________________________________
TABLE 19 ______________________________________ SEQ ID NO: 88 % of Nucleotide in mixture CodeA T G C ______________________________________ J 6 82 6 6 E 82 6 6 6H 1 1 1 97 I 6 6 82 6K 15 15 15 55R 15 55 15 15 ______________________________________
TABLE 20 ______________________________________ SEQ ID NO: 90 % of Nucleotide in mixture CodeA T G C ______________________________________ J 6 82 6 6F 6 6 6 82N 25 25 25 25 E 82 6 6 6 I 6 6 82 6 L 8 1 83 8O 1 1 1 97 ______________________________________
TABLE 21 ______________________________________ SEQ ID NO: 91 % of Nucleotide in mixture CodeA T G C ______________________________________ J 6 82 6 6 E 82 6 6 6H 1 1 1 97 I 6 6 82 6N 25 25 25 25 M 82 2 8 8 ______________________________________
TABLE 22
______________________________________
SEQ ID NO: 92
% of Nucleotide in mixture
Code A T G C
______________________________________
J 6 82 6 6
Q 0 9 82 9
F 6 6 6 82
N 25 25 25 25
E 82 6 6 6
I 6 6 82 6
______________________________________
TABLE 23
______________________________________
SEQ ID NO: 92
% of Nucleotide in mixture
Code A T G C
______________________________________
J 6 82 6 6
F 6 6 6 82
N 25 25 25 25
E 82 6 6 6
I 6 6 82 6
______________________________________
TABLE 24
______________________________________
SEQ ID NO: 95
% of Nucleotide in mixture
Code A T G C
______________________________________
J 6 82 6 6
N 25 25 25 25
E 82 6 6 6
I 6 6 82 6
M 82 2 8 8
P 8 2 8 82
S 1 97 1 1
______________________________________
Atomic Coordinates for Cry3Bb
The atomic coordinates of the Cry3Bb protein are given in the Appendix included in Section 9.1
Atomic Coordinates for Cry3A
The atomic coordinates of the Cry3A protein are given in the Appendix included in Section 9.2
Modification of Cry Genes for Expression in Plants
Wild-type cry genes are known to be expressed poorly in plants as a full length gene or as a truncated gene. Typically, the G+C content of a cry gene is low (37%) and often contains many A+T rich regions, potential polyadenylation sites and numerous ATTTA sequences. Table 25 shows a list of potential polyadenylation sequences which should be avoided when preparing the "plantized" gene construct.
TABLE 25 ______________________________________ LIST OF SEQUENCES OF THE POTENTIAL POLYADENYLATION SIGNALS ______________________________________ AATAAA* AAGCAT AATAAT* ATTAAT AACCAA ATACAT ATATAA AAAATA AATCAA ATTAAA** ATACTA AATTAA** ATAAAA AATACA** ATGAAA CATAAA** ______________________________________ *indicates a potential major plant polyadenylation site. **indicates a potential minor animal polyadenylation site. All others are potential minor plant polyadenylation sites.
The regions for mutagenesis may be selected in the following manner. All regions of the DNA sequence of the cry gene are identified which contained five or more consecutive base pairs which were A or T. These were ranked in terms of length and highest percentage of A+T in the surrounding sequence over a 20-30 base pair region. The DNA is analysed for regions which might contain polyadenylation sites or ATTTA sequences. Oligonucleotides are then designed which maximize the elimination of A+T consecutive regions which contained one or more polyadenylation sites or ATTTA sequences. Two potential plant polyadenylation sites have been shown to be more critical based on published reports. Codons are selected which increase G+C content, but do not generate restriction sites for enzymes useful for cloning and assembly of the modified gene (e.g., BamHI, BglII, SacI, NcoI, EcoRV, etc.). Likewise condons are avoided which contain the doublets TA or GC which have been reported to be infrequently-found codons in plants.
Although the CaMV35S promoter is generally a high level constitutive promoter in most plant tissues, the expression level of genes driven the CaMV35S promoter is low in floral tissue relative to the levels seen in leaf tissue. Because the economically important targets damaged by some insects are the floral parts or derived from floral parts (e.g., cotton squares and bolls, tobacco buds, tomato buds and fruit), it is often advantageous to increase the expression of crystal proteins in these tissues over that obtained with the CaMV35S promoter.
The b 35S promoter of Figwort Mosaic Virus (FMV) is analogous to the CaMV35S promoter. This promoter has been isolated and engineered into a plant transformation vector. Relative to the CaMV promoter, the FMV 35S promoter is highly expressed in the floral tissue, while still providing similar high levels of gene expression in other tissues such as leaf. A plant transformation vector, may be constructed in which the full length synthetic cry gene is driven by the FMV 35S promoter. Tobacco plants may be transformed with the vector and compared for expression of the crystal protein by Western blot or ELISA immunoassay in leaf and floral tissue. The FMV promoter has been used to produce relatively high levels of crystal protein in floral tissue compared to the CaMV promoter.
Expression of Synthetic Cry Genes with ssRUBISCO Promoters and Chloroplast Transit Peptides
The genes in plants encoding the small subunit of RUBISCO (SSU) are often highly expressed, light regulated and sometimes show tissue specificity. These expression properties are largely due to the promoter sequences of these genes. It has been possible to use SSU promoters to express heterologous genes in transformed plants. Typically a plant will contain multiple SSU genes, and the expression levels and tissue specificity of different SSU genes will be different. The SSU proteins are encoded in the nucleus and synthesized in the cytoplasm as precursors that contain an N-terminal extension known as the chloroplast transit peptide (CTP). The CTP directs the precursor to the chloroplast and promotes the uptake of the SSU protein into the chloroplast. In this process, the CTP is cleaved from the SSU protein. These CTP sequences have been used to direct heterologous proteins into chloroplasts of transformed plants.
The SSU promoters might have several advantages for expression of heterologous genes in plants. Some SSU promoters are very highly expressed and could give rise to expression levels as high or higher than those observed with the CaMV35S promoter. The tissue distribution of expression from SSU promoters is different from that of the CaMV35S promoter, so for control of some insect pests, it may be advantageous to direct the expression of crystal proteins to those cells in which SSU is most highly expressed. For example, although relatively constituitive, in the leaf the CaMV35S promoter is more highly expressed in vascular tissue than in some other parts of the leaf, while most SSU promoters are most highly expressed in the mesophyll cells of the leaf. Some SSU promoters also are more highly tissue specific, so it could be possible to utilize a specific SSU promoter to express the protein of the present invention in only a subset of plant tissues, if for example expression of such a protein in certain cells was found to be deleterious to those cells. For example, for control of Colorado potato beetle in potato, it may be advantageous to use SSU promoters to direct crystal protein expression to the leaves but not to the edible tubers.
Utilizing SSU CTP sequences to localize crystal proteins to the chloroplast might also be advantageous. Localization of the B. thuringiensis crystal proteins to the chloroplast could protect these from proteases found in the cytoplasm. This could stabilize the proteins and lead to higher levels of accumulation of active toxin. cry genes containing the CTP could be used in combination with the SSU promoter or with other promoters such as CaMV35S.
Targeting of Cry* Proteins to the Extracellular Space or Vacuole through the Use of Signal Peptides
The B. thuringiensis proteins produced from the synthetic genes described here are localized to the cytoplasm of the plant cell, and this cytoplasmic localization results in plants that are insecticidally effective. It may be advantageous for some purposes to direct the B. thuringiensis proteins to other compartments of the plant cell. Localizing B. thuringiensis proteins in compartments other than the cytoplasm may result in less exposure of the B. thuringiensis proteins to cytoplasmic proteases leading to greater accumulation of the protein yielding enhanced insecticidal activity. Extracellular localization could lead to more efficient exposure of certain insects to the B. thuringiensis proteins leading to greater efficacy. If a B. thuringiensis protein were found to be deleterious to plant cell function, then localization to a noncytoplasmic compartment could protect these cells from the protein.
In plants as well as other eukaryotes, proteins that are destined to be localized either extracellularly or in several specific compartments are typically synthesized with an N-terminal amino acid extension known as the signal peptide. This signal peptide directs the protein to enter the compartmentalization pathway, and it is typically cleaved from the mature protein as an early step in compartmentalization. For an extracellular protein, the secretory pathway typically involves cotranslational insertion into the endoplasmic reticulum with cleavage of the signal peptide occurring at this stage. The mature protein then passes through the Golgi body into vesicles that fuse with the plasma membrane thus releasing the protein into the extracellular space. Proteins destined for other compartments follow a similar path-way. For example, proteins that are destined for the endoplasmic reiculum or the Golgi body follow this scheme, but they are specifically retained in the appropriate compartment. In plants, some proteins are also targeted to the vacuole, another membrane bound compartment in the cytoplasm of many plant cells. Vacuole targeted proteins diverge from the above pathway at the Golgi body where they enter vesicles that fuse with the vacuole.
A common feature of this protein targeting is the signal peptide that initiates the compartmentalization process. Fusing a signal peptide to a protein will in many cases lead to the targeting of that protein to the endoplasmic reticulum. The efficiency of this step may depend on the sequence of the mature protein itself as well. The signals that direct a protein to a specific compartment rather than to the extracellular space are not as clearly defined. It appears that many of the signals that direct the protein to specific compartments are contained within the amino acid sequence of the mature protein. This has been shown for some vacuole targeted proteins, but it is not yet possible to define these sequences precisely. It appears that secretion into the extracellular space is the "default" pathway for a protein that contains a signal sequence but no other compartmentalization signals. Thus, a strategy to direct B. thuringiensis proteins out of the cytoplasm is to fuse the genes for synthetic B. thuringiensis genes to DNA sequences encoding known plant signal peptides. These fusion genes will give rise to B. thuringiensis proteins that enter the secretory pathway, and lead to extracellular secretion or targeting to the vacuole or other compartments. Signal sequences for several plant genes have been described. One such sequence is for the tobacco pathogenesis related protein PR1b has been previously described (Cornelissen et al, 1986). The PR1b protein is normally localized to the extracellular space. Another type of signal peptide is contained on seed storage proteins of legumes. These proteins are localized to the protein body of seeds, which is a vacuole like compartment found in seeds. A signal peptide DNA sequence for the β-subunit of the 7S storage protein of common bean (Phaseolus vulgaris), PvuB has been described (Doyle et al., 1986). Based on the published these published sequences, genes may be synthesized chemically using oligonucleotides that encode the signal peptides for PRlb and PvuB. In some cases to achieve secretion or compartmentalization of heterologous proteins, it may be necessary to include some amino acid sequence beyond the normal cleavage site of the signal peptide. This may be necessary to insure proper cleavage of the signal peptide.
Isolation of Transgenic Maize Resistant to Diabrotica spp. Using Cry3Bb Variants
The expression of a plant gene which exists in double-stranded DNA form involves transcription of messenger RNA (mRNA) from one strand of the DNA by RNA polymerase enzyme, and the subsequent processing of the mRNA primary transcript inside the nucleus. This processing involves a 3' non-translated region which adds polyadenylate nucleotides to the 3' end of the RNA. Transcription of DNA into mRNA is regulated by a region of DNA usually referred to as the "promoter". The promoter region contains a sequence of bases that signals RNA polymerase to associate with the DNA and to initiate the transcription of mRNA using one of the DNA strands as a template to make a corresponding strand of RNA.
A number of promoters which are active in plant cells have been described in the literature. Such promoters may be obtained from plants or plant viruses and include, but are not limited to, the nopaline synthase (NOS) and octopine synthase (OCS) promoters (which are carried on tumor-inducing plasmids of Agrobacterium tumefaciens), the cauliflower mosaic virus (CaMV) 19S and 35S promoters, the light-inducible promoter from the small subunit of ribulose 1,5-bisphosphate carboxylase (ssRUBISCO, a very abundant plant polypeptide), and the Figwort Mosaic Virus (FMV) 35S promoter. All of these promoters have been used to create various types of DNA constructs which have been expressed in plants (see e.g., U.S. Pat. No. 5,463,175, specifically incorporated herein by reference).
The particular promoter selected should be capable of causing sufficient expression of the enzyme coding sequence to result in the production of an effective amount of protein. One set of preferred promoters are constitutive promoters such as the CaMV35S or FMV35S promoters that yield high levels of expression in most plant organs (U.S. Pat. No. 5,378,619, specifically incorporated herein by reference). Another set of preferred promoters are root enhanced or specific promoters such as the CaMV derived 4 as-1 promoter or the wheat POX1 promoter (U.S. Pat. No. 5,023,179, specifically incorporated herein by reference; Hertig et al., 1991). The root enhanced or specific promoters would be particularly preferred for the control of corn rootworm (Diabroticus spp.) in transgenic corn plants.
The promoters used in the DNA constructs (i.e. chimeric plant genes) of the present invention may be modified, if desired, to affect their control characteristics. For example, the CaMV35S promoter may be ligated to the portion of the ssRUBISCO gene that represses the expression of ssRUBISCO in the absence of light, to create a promoter which is active in leaves but not in roots. The resulting chimeric promoter may be used as described herein. For purposes of this description, the phrase "CaMV35S" promoter thus includes variations of CaMV35S promoter, e.g, promoters derived by means of ligation with operator regions, random or controlled mutagenesis, etc. Furthermore, the promoters may be altered to contain multiple "enhancer sequences" to assist in elevating gene expression.
The RNA produced by a DNA construct of the present invention also contains a 5' non-translated leader sequence. This sequence can be derived from the promoter selected to express the gene, and can be specifically modified so as to increase translation of the mRNA. The 5' non-translated regions can also be obtained from viral RNA's, from suitable eucaryotic genes, or from a synthetic gene sequence. The present invention is not limited to constructs wherein the non-translated region is derived from the 5' non-translated sequence that accompanies the promoter sequence.
For optimized expression in monocotyledenous plants such as maize, an intron should also be included in the DNA expression construct. This intron would typically be placed near the 5' end of the mRNA in untranslated sequence. This intron could be obtained from, but not limited to a set of introns consisting of the maize hsp70 intron (U.S. Pat. No. 5,424,412; specifically incorporated herein by reference) or the rice Act1 intron (McElroy et al., 1990). As shown below, the maize hsp70 intron is useful in the present invention.
As noted above, the 3' non-translated region of the chimeric plant genes of the present invention contains a polyadenylation signal which functions in plants to cause the addition of adenylate nucleotides to the 3' end of the RNA. Examples of preferred 3' regions are (1) the 3' transcribed, non-translated regions containing the polyadenylate signal of Agrobacterium tumor-inducing (Ti) plasmid genes, such as the nopaline synthase (NOS) gene and (2) plant genes such as the pea ssRUBISCO E9 gene (Fischhoffet al., 1987).
A chimeric plant gene containing a structural coding sequence of the present invention can be inserted into the genome of a plant by any suitable method. Suitable plant transformation vectors include those derived from a Ti plasmid of Agrobacterium tumefaciens, as well as those disclosed, e.g., by Herrera-Estrella (1983), Bevan (1983), Klee (1985) and Eur. Pat. Appl. Publ. No. EP0120516. In addition to plant transformation vectors derived from the Ti or root-inducing (Ri) plasmids of Agrobacterium, alternative methods can be used to insert the DNA constructs of this invention into plant cells. Such methods may involve, for example, the use of liposomes, electroporation, chemicals that increase free DNA uptake, free DNA delivery via microprojectile bombardment, and transformation using viruses or pollen (Fromm et al., 1986; Armstrong et al., 1990; Fromm et a., 1990).
For efficient expression of the cry3Bb variants in transgenic plants, the gene encoding the variants must have a suitable sequence composition (Diehn et al., 1996). One example of such a sequence is shown for the v11231 gene (SEQ ID NO:99) which encodes the Cry3Bb11231 variant protein (SEQ ID NO:100) with Diabrotica activity. This gene was derived via mutagenesis (Kunkel, 1985) of a cry3Bb synthetic gene (SEQ ID NO:101) encoding a protein essentially homologous to the protein encoded by the native cry3Bb gene (Gen Bank Accession Number m89794, SEQ ID NO:102). The following oligonucleotides were used in the mutagenesis of the original cry3Bb synthetic gene (SEQ ID NO:101) to create the v11231 gene (SEQ ID NO:99):
Oligo #1:
5'-TAGGCCTCCATCCATGGCAAACCCTAACAATC-3' (SEQ ID NO:103)
Oligo #2:
5'-TCCCATCTTCCTACTTACGACCCTGCAGAAATACGGTCCAAC -3' (SEQ ID NO:104)
Oligo #3:
5'-GACCTCACCTACCAAACATTCGATCTTG-3' (SEQ ID NO:105)
Oligo #4:
5'-CGAGTTCTACCGTAGGCAGCTCAAG-3' (SEQ ID NO:106)
To place the cry3Bb variant gene v11231 in a vector suitable for expression in monocotyledonous plants (i.e. under control of the enhanced Cauliflower Mosaic Virus 35S promoter and link to the hsp70 intron followed by a nopaline synthase polyadenylation site as in U.S. Pat. No. 5,424,412, specifically incorporated herein by reference), the vector pMON19469 was digested with NcoI and EcoRI. The larger vector band of approximately 4.6 kb was electrophoresed, purified, and ligated with T4 DNA ligase to the NcoI-EcoRI fragment of approximately 2 kb containing the v11231 gene (SEQ ID NO:99). The ligation mix was transformed into E. coli, carbenicillin resistant colonies recovered and plasmid DNA recovered by DNA miniprep procedures. This DNA was subjected to restriction endonuclease analysis with enzymes such as NcoI and EcoRI (together), NotI, and PstI to identify clones containing pMON33708 (the v11231 coding sequence fused to the hsp70 intron under control of the enhanced CaMV35S promoter).
To place the v11231 gene in a vector suitable for recovery of stably transformed and insect resistant plants, the 3.75-kb NotI restriction fragment from pMON33708 containing the lysine oxidase coding sequence fused to the hsp70 intron under control of the enhanced CaMV35S promoter was isolated by gel electrophoresis and purification. This fragment was ligated with pMON30460 treated with NotI and calf intestinal alkaline phosphatase (pMON30460 contains the neomycin phosphotransferase coding sequence under control of the CaMV35S promoter). Kanamycin resistant colonies were obtained by transformation of this ligation mix into E. coli and colonies containing pMON33710 identified by restriction endonuclease digestion of plasmid miniprep DNAs. Restriction enzymes such as NotI, EcoRV, HindIII, NcoI, EcoRI, and BglII can be used to identify the appropriate clones containing the NotI fragment of pMON33708 in the NotI site of pMON30460 (i.e. pMON33710) in the orientation such that both genes are in tandem (i.e. the 3' end of the v11231 expression cassette is linked to the 5' end of the nptII expression cassette). Expression of the v11231 protein by pMON33710 in corn protoplasts was confirmed by electroporation of pMON33710 DNA into protoplasts followed by protein blot and ELISA analysis. This vector can be introduced into the genomic DNA of corn embryos by particle gun bombardment followed by paromomycin selection to obtain corn plants expressing the v11231 gene essentially as described in U.S. Pat. No. 5,424,412, specifically incorporated herein by reference.
In this example, the vector was introduced via cobombardment with a hygromycin resistance conferring plasmid into immature embryo scutella (IES) of maize, followed by hygromycin selection, and regeneration. Transgenic corn lines expressing the v11231 protein were identified by ELISA analysis. Progeny seed from these events were subsequently tested for protection from Diabrotica feeding.
Transformed corn plants expressing Cry3Bb.11231 protein were challenged with western corn rootworm (WCR) larvae in both a seedling and 10 inch pot assay. The transformed genotype was A634, where the progeny of the RO cross by A634 was evaluated. Observations included effect on larval development (weight), root damage rating (RDR), and protein expression. The transformation vector containing the cry3Bb gene was pMON33710. Treatments included the positive and negative iso-populations for each event and an A634 check.
The seedling assay consisted of the following steps: (i) single seeds were placed in 1 oz cups containing potting soil; (ii) at spiking, each seedling was infested with 4 neonate larvae; and (iii) after infestation, seedlings were incubated for 7 days at 25° C., 50% RH, and 14:10 (L:D) photo period. Adequate moisture was added to the potting soil during the incubation period to maintain seedling vigor.
The 10 inch pot assay consisted of the following steps: (i) single seeds were placed in 10 inch pots containing potting soil; (ii) at 14 days post planting, each pot was infested with 800 eggs which have been pre-incubated such that hatch would occur 5-7 days post infestation; and (iii) after infestation, plants were incubated for 4 weeks under the same environmental conditions as the seedling assay. Pots were both sub and top irrigated daily.
For the seedling assay, on day 7 plants were given a root damage rating, and surviving larvae were weighed. Also at this time, Cry3Bb protein concentrations in the roots were determined by ELISA. The scale used for the seedling assay to assess root damage is as follows: RDR (root damage rating) 0=no visible feeding; RDR 1=very light feeding; RDR 2=light feeding; RDR 3=moderate feeding; RDR 4=heavy feeding; and RDR 5 =very heavy feeding.
Results of the seedling assay are shown in Table 26. Plants expressing Cry3Bb protein were completely protected by WCR feeding, where surviving larvae within this treatment had not grown. Mean larval weights ranged from 2.03-2.73 mg for the nonexpressing treatments, where the surviving larval average weight was 0.11 mg on the expressing cry3Bb treatment. Root damage ratings were 3.86 and 0.33 for the nonexpressing and expressing isopopulations, respectively. Larval survival ranged from 75-85% for the negative and check treatments, where only 25% of the larvae survived on the Cry3Bb treatment.
TABLE 26
______________________________________
EFFECT OF CRY3BB EXPRESSING PLANTS ON
WCR LARVAE IN A SEEDLING ASSAY
Plants Larvae
Root % Mean ± SD
Event
Treatment
N (ppm) RDR ± SD
N Surv Wt. (mg)
______________________________________
16 Negative 7 0.0 3.86 ± 0.65
21 75 2.73 ± 1.67
16 Positive 3 29.01 0.33 ± 0.45
3 25 0.11 ± 0.07
A634 Check 4 0.0 -- 13 81 2.03 ± 0.83
______________________________________
For the 10 inch pot assay, at 4 weeks post infestation plant height was recorded and a root damage rating (Iowa 1-6 scale; Hills and Peters, 1971) was given.
Results of the 10 inch pot assay are shown in Table 27. Plants expressing Cry3Bb protein had significantly less feeding damage and were taller than the non-expressing plants. Event 16, the higher of the two expressing events provided nearly complete control. The negative treatments had very high root damage ratings indicating very high insect pressure. The positive mean root damage ratings were 3.4 and 2.2 for event 6 and 16, respectively. Mean RDR for the negative treatment was 5.0 and 5.6.
TABLE 27
______________________________________
EFFECT OF CRY3BB EXPRESSING CORN IN CONTROLLING
WCR LARVAL FEEDING IN A 10 INCH POT ASSAY
Root Plant Height
Event Treatment
N (ppm) RDR ± SD
(cm)
______________________________________
6 Negative 7 0.0 5.0 ± 1.41
49.7 ± 18.72
6 Positive 5 7.0 3.4 ± 1.14
73.9 ± 8.67
16 Negative 5 0.0 5.6 ± 0.89
61.2 ± 7.75
16 Positive 5 55.0 2.2 ± 0.84
83.8 ± 7.15
______________________________________
In summary, corn plants expressing Cry3Bb protein have a significant biological effect on WCR larval development as seen in the seedling assay. When challenged with very high infestation levels, plants expressing the Cry3Bb protein were protected from WCR larval feeding damage as illustrated in the 10 inch pot assay.
SEQ ID NO:1 DNA sequence of cry3Bb.11221 gene.
SEQ ID NO:2 Amino acid sequence of Cry3Bb.11221 polypeptide.
SEQ ID NO:3 DNA sequence of cry3Bb.11222 gene.
SEQ ID NO:4 Amino acid sequence of Cry3Bb.11222 polypeptide.
SEQ ID NO:5 DNA sequence of cry3Bb.11223 gene.
SEQ ID NO:6 Amino acid sequence of Cry3Bb.11223 polypeptide.
SEQ ID NO:7 DNA sequence of cry3Bb.11224 gene.
SEQ ID NO:8 Amino acid sequence of Cry3Bb.11224 polypeptide.
SEQ ID NO:9 DNA sequence of cry3Bb.11225 gene.
SEQ ID NO:10 Amino acid sequence of Cry3Bb.11225 polypeptide.
SEQ ID NO:11 DNA sequence of cry3Bb.11226 gene.
SEQ ID NO:12 Amino acid sequence of Cry3Bb.11226 polypeptide.
SEQ ID NO:13 DNA sequence of cry3Bb.11227 gene.
SEQ ID NO:14 Amino acid sequence of Cry3Bb.11227 polypeptide.
SEQ ID NO:15 DNA sequence of cry3Bb.11228 gene.
SEQ ID NO:16 Amino acid sequence of Cry3Bb.11228 polypeptide.
SEQ ID NO:17 DNA sequence of cry3Bb.11229 gene.
SEQ ID NO:18 Amino acid sequence of Cry3Bb.11229 polypeptide.
SEQ ID NO:19 DNA sequence of cry3Bb.11230 gene.
SEQ ID NO:20 Amino acid sequence of Cry3Bb.11230 polypeptide.
SEQ ID NO:21 DNA sequence of cry3Bb.11231 gene.
SEQ ID NO:22 Amino acid sequence of Cry3Bb.11231 polypeptide.
SEQ ID NO:23 DNA sequence of cry3Bb.11232 gene.
SEQ ID NO:24 Amino acid sequence of Cry3Bb.11232 polypeptide.
SEQ ID NO:25 DNA sequence of cry3Bb.11233 gene.
SEQ ID NO:26 Amino acid sequence of Cry3Bb.11233 polypeptide.
SEQ ID NO:27 DNA sequence of cry3Bb.11234gene.
SEQ ID NO:28 Amino acid sequence of Cry3Bb.11234 polypeptide.
SEQ ID NO:29 DNA sequence of cry3Bb.1235 gene.
SEQ ID NO:30 Amino acid sequence of Cry3Bb.11235 polypeptide.
SEQ ID NO:31 DNA sequence of cry3Bb.1236 gene.
SEQ ID NO:32 Amino acid sequence of Cry3Bb.11236 polypeptide.
SEQ ID NO:33 DNA sequence of cry3Bb.11237 gene.
SEQ ID NO:34 Amino acid sequence of Cry3Bb.11237 polypeptide.
SEQ ID NO:35 DNA sequence of cry3Bb.1238 gene.
SEQ ID NO:36 Amino acid sequence of Cry3Bb.11238 polypeptide.
SEQ ID NO:37 DNA sequence of cry3Bb.11239 gene.
SEQ ID NO:38 Amino acid sequence of Cry3Bb.11239 polypeptide.
SEQ ID NO:39 DNA sequence of cry3Bb.11241 gene.
SEQ ID NO:40 Amino acid sequence of Cry3Bb.11241 polypeptide.
SEQ ID NO:41 DNA sequence of cry3Bb.11242 gene.
SEQ ID NO:42 Amino acid sequence of Cry3Bb.11242 polypeptide.
SEQ ID NO:43 DNA sequence of cry3Bb.11032 gene.
SEQ ID NO:44 Amino acid sequence of Cry3Bb.11032 polypeptide.
SEQ ID NO:45 DNA sequence of cry3Bb.11035 gene.
SEQ ID NO:46 Amino acid sequence of Cry3Bb.11035 polypeptide.
SEQ ID NO:47 DNA sequence of cry3Bb.11036 gene.
SEQ ID NO:48 Amino acid sequence of Cry3Bb.11036 polypeptide.
SEQ ID NO:49 DNA sequence of cry3Bb.11046 gene.
SEQ ID NO:50 Amino acid sequence of Cry3Bb.11046 polypeptide.
SEQ ID NO:51 DNA sequence of cry3Bb.11048 gene.
SEQ ID NO:52 Amino acid sequence of Cry3Bb.11048 polypeptide.
SEQ ID NO:53 DNA sequence of cry3Bb.11051 gene.
SEQ ID NO:54 Amino acid sequence of Cry3Bb.11051 polypeptide.
SEQ ID NO:55 DNA sequence of cry3Bb.11057 gene.
SEQ ID NO:56 Amino acid sequence of Cry3Bb.11057 polypeptide.
SEQ ID NO:57 DNA sequence of cry3Bb.11058 gene.
SEQ ID NO:58 Amino acid sequence of Cry3Bb.11058 polypeptide.
SEQ ID NO:59 DNA sequence of cry3Bb.11081 gene.
SEQ ID NO:60 Amino acid sequence of Cry3Bb.11081 polypeptide.
SEQ ID NO:61 DNA sequence of cry3Bb.11082 gene.
SEQ ID NO:62 Amino acid sequence of Cry3Bb.11082 polypeptide.
SEQ ID NO:63 DNA sequence of cry3Bb.11083 gene.
SEQ ID NO:64 Amino acid sequence of Cry3Bb.11083 polypeptide.
SEQ ID NO:65 DNA sequence of cry3Bb.11084 gene.
SEQ ID NO:66 Amino acid sequence of Cry3Bb.11084 polypeptide.
SEQ ID NO:67 DNA sequence of cry3Bb.11095 gene.
SEQ ID NO:68 Amino acid sequence of Cry3Bb.11095 polypeptide.
SEQ ID NO:69 DNA sequence of cry3Bb.60 gene.
SEQ ID NO:70 Amino acid sequence of Cry3Bb.60 polypeptide.
SEQ ID NO:71 Primer FW001.
SEQ ID NO:72 Primer FW006.
SEQ ID NO:73 Primer MVT095.
SEQ ID NO:74 Primer MVT097.
SEQ ID NO:75 Primer MVT091.
SEQ ID NO:76 Primer MVT075.
SEQ ID NO:77 Primer MVT076.
SEQ ID NO:78 Primer MVT111.
SEQ ID NO:79 Primer MVT094.
SEQ ID NO:80 Primer MVT103.
SEQ ID NO:81 Primer MVT081.
SEQ ID NO:82 Primer MVT085.
SEQ ID NO:83 Primer A.
SEQ ID NO:84 Primer B.
SEQ ID NO:85 Primer C.
SEQ ID NO:86 Primer D.
SEQ ID NO:87 Primer E.
SEQ ID NO:88 Primer F.
SEQ ID NO:89 Primer G.
SEQ ID NO:90 Primer WD112.
SEQ ID NO:91 Primer WD115.
SEQ ID NO:92 Primer MVT105.
SEQ ID NO:93 Primer MVT092.
SEQ ID NO:94 Primer MVT070.
SEQ ID NO:95 Primer MVT083.
SEQ ID NO:96 N-terminal amino acid of Cry3Bb polypeptide.
SEQ ID NO:97 DNA sequence of wild-type cry3Bb gene.
SEQ ID NO:98 Amino acid sequence of wild-type Cry3Bb polypeptide.
SEQ ID NO:99 Plantized DNA sequence for cry3Bb.11231 gene.
SEQ ID NO:100 Amino acid sequence of plantized Cry3Bb.11231 polypeptide.
SEQ ID NO:101 DNA sequence of cry3Bb gene used to prepare SEQ ID NO:99.
SEQ ID NO:102 DNA sequence of wild-type cry3Bb gene, Genbank #M89794.
SEQ ID NO:103 DNA sequence of Oligo # 1.
SEQ ID NO:104 DNA sequence of Oligo # 2.
SEQ ID NO:105 DNA sequence of Oligo # 3.
SEQ ID NO:106 DNA sequence of Oligo # 4.
SEQ ID NO:107 DNA sequence of cry3Bb.11098 gene.
SEQ ID NO:108 Amino acid sequence of Cry3Bb.11098 polypeptide.
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__________________________________________________________________________ 8.0 APPENDIX __________________________________________________________________________ 8.1 CRYSTAL COORDINATES OF CRY3BB HEADER TOXIN 01-DEC-94 COMPND DELTA ENDOTOXIN CRYIIIB2 SOURCE (BACILLUS THURINGIENSIS, SUBSPECIES KUMAMOTOENSIS) AUTHOR N. GALITSKY,V. CODY REVDAT 1 01-DEC-94REMARK 1REMARK 1REFERENCE 1REMARK 1 AUTH NIKOLAI GALITSKY, VIVIAN CODY, ANDREZEJ WOJTCZAK, REMARKS 1 AUTH DEBASHIS GHOSH, JOSEPH R. LUFT, WALTER PANGBORN, REMARKS 1 AUTH ZDZISLAW WAWRZAK AND LEIGH ENGLISH.REMARK 1 TITL CRYSTAL AND MOLECULAR STRUCTURE OF THEBACTERIRIAL REMARK 1TITL 2 DELTA-ENDOTOXIN CRYIIIB2.REMARK 1REF REMARK 1REFN REMARK 1REFERENCE 2REMARK 1 AUTH CODY, V., LUFT, J. R., JENSEN, E., PANGBORG, W., & REMARKS 1 AUTH ENGLISH,L. REMARK 1 TITL PURIFICATION AND CRYSTALLIZATION OF INSECTICIDAL REMARKS 1TITL 1 DELTA-ENDOTOXIN CRYIIIB2 FROMBACILLUS THURINGIENSIS REMARK 1 REF PROTEINS: STRUC. FUNC. GENETICS, (1992), 14, 324.REMARK 2REMARK 2REMARK 2 RESOLUTION. 2.4 ANGSTROMS.REMARK 3REMARK 3REMARK 3 REFINEMENT.REMARK 3PROGRAM X-PLOR REMARK 3 AUTHORS BRUNGER REMARK 3 R VALUE 0.18REMARK 3 RFREE VALUE 0.253REMARK 3 RMSD BOND DISTANCES 0.009ANGSTROMS REMARK 3 RMSD BOND ANGLES 1.30DEGREES REMARK 3REMARK 3 NUMBER OF REFLECTIONS 29069REMARK 3 RESOLUTION RANGE 8.0-2.4ANGSTROMS REMARK 3 DATA CUTOFF 2.0 SIGMA(F)REMARK 3REMARK 3 NUMBER OF PROTEIN ATOMS 4750REMARK 3 NUMBER OF SOLVENT ATOMS 251REMARK 3REMARK 3 THE ATOMIC MODEL INCLUDES RESIDUES 64-652 OF THEPROTEIN REMARK 3 AND 251 BOUND WATER MOLECULES.REMARK 3REMARK 4REMARK 4 Bacllius thuringiensis (Bt) is a gram-positive soil REMARK 4 bacterium characterized by its ability to produceREMARK 4 crystalline inclusions during sporulation which consist ofREMARK 4 proteins exhibiting a highly specificinsecticidal activity REMARK 4 There are a variety of toxins present in Bt which haveREMARK 4 different charactistics, for example, a-exotoxin REMARK 4 (phospholipase C) and d-endotoxin (the crystal protein).REMARK 4REMARK 5REMARK 6REMARK 6 HERE RESULTED FROM LAST REFINEMENT. REMARK 6 R = 18.0%, Rfree = 24.3% byX-PLOR REMARK 6SEQRES 1 ASP ALA VAL GLY THR GLY ILE SER VAL VAL GLYGLN ILE SEQRES 2 LEU GLY VAL VAL GLY VAL PRO PHE ALA GLY ALALEU THR SEQRES 3 SER PHE TYR GLN SER PHE LEU ASN THR ILE TRP PRO SER SEQRES 4 ASP ALA ASP PRO TRP LYS ALA PHE MET ALA GLN VAL GLU SEQRES 5 VAL LEU ILE ASP LYS LYS ILE GLU GLU TYR ALA LYS SER SEQRES 6 LYS ALA LEU ALA GLU LEU GLN GLY LEU GLN ASN ASN PHE SEQRES 7 GLU ASP TYR TYR VAL ASN VAL LEU ASN TRP LYS LYS THR SEQRES 8 PRO LEU SER LEU ARG SER LYS ARG SER GLN ASP ARG ILE SEQRES 9 ARG GLU LEU PHE SER GLN ALA GLU SER HIS PHE PHE ARG SEQRES 10 ASN SER MET PRO SER PHE ALA VAL SER LYS PHE GLU VAL SEQRES 11 LEU PHE LEU PRO THR TYR ALA GLN ALA ALA ASN THR HIS SEQRES 12 LEU LEU LEU LEU LYS ASP ALA GLN VAL PHE GLY GLU GLU SEQRES 13 TRP GLY TYR SER SER GLU ASP VAL ALA GLU PHE TYR HIS SEQRES 14 ARG GLN LEU LYS LEU THR GLN GLN TYR THR ASP HIS CYS SEQRES 15 VAL ASP TRP TYR ASN VAL GLY LEU ASN GLY LEU ARG GLY SEQRES 16 SER THR TYR ASP ALA TRP VAL LYS PHE ASN ARG PHE ARG SEQRES 17 ARG GLU MET THR LEU THR VAL LEU ASP LEU ILE VAL LEU SEQRES 18 PHE PRO PHE TYR ASP ILE ARG LEU TYR SER LYS GLY VAL SEQRES 19 LYS THR GLU LEU THR ARG ASP ILE PHE THR ASP PRO ILE SEQRES 20 PHE SER ILE ASN THR LEU GLN GLU TYR GLY PRO THR PHE SEQRES 21 LEU SER ILE GLU ASN SER ILE ARG LYS PRO HIS LEU PHE SEQRES 22 ASP TYR LEU GLN GLY ILE GLU PHE THR ARG LEU GLN PRO SEQRES 23 GLY TYR PHE GLY LYS ASP SER PHE ASN TYR TRP SER GLY SEQRES 24 ASN TYR VAL GLU THR ARG PRO SER ILE GLY SER SER LYS SEQRES 25 THR ILE THR SER PRO PHE TYR GLY ASP LYS SER THR GLU SEQRES 26 PRO VAL GLN LYS LEU SER PHE ASP GLY GLN LYS VAL TYR SEQRES 27 ARG THR ILE ALA ASN THR ASP VAL ALA ALA TRP PRO ASN SEQRES 28 GLY LYS VAL TYR LEU GLY VAL THR LYS VAL ASP PHE SER SEQRES 29 GLN TYR ASP ASP GLN LYS ASN GLU THR SER THR GLN THR SEQRES 30 TYR ASP SER LYS ARG ASN ASN GLY HIS VAL SER ALA GLN SEQRES 31 ASP SER ILE ASP GLN LEU PRO PRO GLU THR THR ASP GLU SEQRES 32 PRO LEU GLU LYS ALA TYR SER HIS GLN LEU ASN TYR ALA SEQRES 33 GLU CYS PHE LEU MET GLN ASP ARG ARG GLY THR ILE PRO SEQRES 34 PHE PHE THR TRP THR HIS ARG SER VAL ASP PHE PHE ASN SEQRES 35 THR ILE ASP ALA GLU LYS ILE THR GLN LEU PRO VAL VAL SEQRES 36 LYS ALA TYR ALA LEU SER SER GLY ALA SER ILE ILE GLU SEQRES 37 GLY PRO GLY PHE THR GLY GLY ASN LEU LEU PHE LEU LYS SEQRES 38 GLU SER SER ASN SER ILE ALA LYS PHE LYS VAL THR LEU SEQRES 39 ASN SER ALA ALA LEU LEU GLN ARG TYR ARG VAL ARG ILE SEQRES 40 ARG TYR ALA SER THR THR ASN LEU ARG LEU PHE VAL GLN SEQRES 41 ASN SER ASN ASN ASP PHE LEU VAL ILE TYR ILE ASN LYS SEQRES 42 THR MET ASN LYS ASP ASP ASP LEU THR TYR GLN THR PHE SEQRES 43 ASP LEU ALA THR THR ASN SER ASN MET GLY PHE SER GLY SEQRES 44 ASP LYS ASN GLU LEU ILE ILE GLY ALA GLU SER PHE VAL SEQRES 45 SER ASN GLU LYS ILE TYR ILE ASP LYS ILE GLU PHE ILE SEQRES 46 PRO VAL GLN LEU CRYST1 122.440 131.810 105.370 90.00 90.00 90.00C 2 2 21 8 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.00817 0.00000 0.000000 0.00000 SCALE2 0.00000 0.00759 0.00000 0.00000 SCALE3 0.00000 0.00000 0.00949 0.00000 ATOM 1 CB ASP 64 38.002 27.615 24.114 1.00 41.41 ATOM 2 CG ASP 64 36.543 27.914 23.755 1.00 52.75 ATOM 3 OD1 ASP 64 35.629 27.527 24.530 1.00 57.53 ATOM 4 OD2 ASP 64 36.313 28.570 22.707 1.00 55.49 ATOM 5 C ASP 64 38.189 25.132 23.609 1.00 31.24 ATOM 6 O ASP 64 39.200 24.940 22.931 1.00 32.62 ATOM 7 N ASP 64 39.547 26.161 25.357 1.00 28.94 ATOM 8 CA ASP 64 38.204 26.213 24.712 1.00 33.24 ATOM 9 N ALA 65 37.061 24.450 23.398 1.00 26.88 ATOM 10 CA ALA 65 37.015 23.396 22.384 1.00 24.54 ATOM 11 CB ALA 65 35.695 22.650 22.456 1.00 25.47 ATOM 12 C ALA 65 37.289 23.923 20.965 1.00 24.59 ATOM 13 O ALA 65 38.208 23.470 20.298 1.00 28.06 ATOM 14 N VAL 66 36.549 24.933 20.533 1.00 24.47 ATOM 15 CA VAL 66 36.756 25.504 19.203 1.00 23.48 ATOM 16 CB VAL 66 35.728 26.617 18.903 1.00 21.61 ATOM 17 CG1 VAL 66 36.030 27.331 17.611 1.00 22.39 ATOM 18 CG2 VAL 66 34.351 25.996 18.820 1.00 26.75 ATOM 19 C VAL 66 38.187 26.004 19.045 1.00 19.98 ATOM 20 O VAL 66 38.833 25.670 18.077 1.00 23.77 ATOM 21 N GLY 67 38.713 26.713 20.034 1.00 21.48 ATOM 22 CA GLY 67 40.081 27.219 19.954 1.00 20.29 ATOM 23 C GLY 67 41.138 26.133 19.879 1.00 24.27 ATOM 24 O GLY 67 42.192 26.309 19.265 1.00 23.94 ATOM 25 N THR 68 40.866 25.002 20.515 1.00 24.20 ATOM 26 CA THR 68 41.799 23.896 20.492 1.00 24.14 ATOM 27 CB THR 68 41.461 22.851 21.597 1.00 23.58 ATOM 28 OG1 THR 68 41.688 23.440 22.875 1.00 31.21 ATOM 29 CG2 THR 68 42.340 21.613 21.500 1.00 27.97 ATOM 30 C THR 68 41.694 23.304 19.103 1.00 20.97 ATOM 31 O THR 68 42.705 23.072 18.454 1.00 21.45 ATOM 32 N GLY 69 40.461 23.174 18.618 1.00 19.58 ATOM 33 CA GLY 69 40.215 22.622 17.293 1.00 19.83 ATOM 34 C GLY 69 40.958 23.401 16.229 1.00 21.30 ATOM 35 O GLY 69 41.668 22.836 15.387 1.00 27.17 ATOM 36 N ILE 70 40.803 24.714 16.292 1.00 17.89 ATOM 37 CA ILE 70 41.439 25.637 15.380 1.00 14.96 ATOM 38 CB ILE 70 40.985 27.081 15.669 1.00 10.04 ATOM 39 CG2 ILE 70 41.955 28.068 15.070 1.00 12.80 ATOM 40 CG1 ILE 70 39.577 27.287 15.087 1.00 17.46 ATOM 41 CD1 ILE 70 38.902 28.609 15.424 1.00 11.32 ATOM 42 C ILE 70 42.941 25.539 15.476 1.00 15.70 ATOM 43 O ILE 70 43.620 25.618 14.480 1.00 14.84 ATOM 44 N SER 71 43.456 25.322 16.675 1.00 20.78 ATOM 45 CA SER 71 44.886 25.235 16.865 1.00 21.23 ATOM 46 CB SER 71 45.203 25.328 18.342 1.00 27.06 ATOM 47 OG SER 71 46.602 25.359 18.562 1.00 38.25 ATOM 48 C SER 71 45.472 23.958 16.271 1.00 21.51 ATOM 49 O SER 71 46.528 23.993 15.34 1.00 25.89 ATOM 50 N VAL 72 44.800 22.835 16.494 1.00 22.02 ATOM 51 CA VAL 72 45.234 21.543 15.966 1.00 21.27 ATOM 52 CB VAL 72 44.307 20.400 16.439 1.00 18.56 ATOM 53 CG1 VAL 72 44.732 19.096 15.847 1.00 23.45 ATOM 54 CG2 VAL 72 44.350 20.282 17.908 1.00 24.48 ATOM 55 C VAL 72 45.230 21.580 14.431 1.00 22.84 ATOM 56 O VAL 72 46.224 21.210 13.806 1.00 26.65 ATOM 57 N VAL 73 44.127 22.028 13.822 1.00 19.72 ATOM 58 CA VAL 73 44.050 22.105 12.359 1.00 20.44 ATOM 59 CB VAL 73 42.619 22.492 11.872 1.00 20.13 ATOM 60 CG1 VAL 73 42.619 22.896 10.378 1.00 13.81 ATOM 61 CG2 VAL 73 41.680 21.308 12.095 1.00 18.37 ATOM 62 C VAL 73 45.152 22.995 11.752 1.00 20.22 ATOM 63 O VAL 73 45.557 22.797 10.615 1.00 24.33 ATOM 64 N GLY 74 45.663 23.939 12.532 1.00 21.00 ATOM 65 CA GLY 74 46.743 24.784 12.072 1.00 16.98 ATOM 66 C GLY 74 48.049 24.028 12.226 1.00 20.80 ATOM 67 O GLY 74 48.950 24.221 11.434 1.00 23.14 ATOM 68 N GLN 75 48.183 23.179 13.247 1.00 22.46 ATOM 69 CA GLN 75 49.438 22.410 13.434 1.00 25.26 ATOM 70 CB GLN 75 49.561 21.810 14.856 1.00 27.10 ATOM 71 CG GLN 75 49.713 22.859 15.996 1.00 29.45 ATOM 72 CD GLN 75 50.044 22.259 17.361 1.00 31.13 ATOM 73 OE1 GLN 75 51.122 21.706 17.557 1.00 40.11 ATOM 74 NE2 GLN 75 49.140 22.408 18.320 1.00 30.96 ATOM 75 C GLN 75 49.566 21.308 12.389 1.00 24.92 ATOM 76 O GLN 75 50.629 21.109 11.793 1.00 26.68 ATOM 77 N ILE 76 48.466 20.601 12.159 1.00 23.54 ATOM 78 CA ILE 76 48.432 19.541 11.174 1.00 23.61 ATOM 79 CB ILE 76 47.092 18.760 11.249 1.00 22.99 ATOM 80 CG2 ILE 76 47.186 17.503 10.408 1.00 26.43 ATOM 81 CG1 ILE 76 46.744 18.375 12.700 1.00 19.22 ATOM 82 CD1 ILE 76 47.392 17.129 13.202 1.00 12.10 ATOM 83 C ILE 76 48.659 20.118 9.733 1.00 24.28 ATOM 84 O ILE 76 49.445 19.557 8.968 1.00 25.09 ATOM 85 N LEU 77 48.004 21.224 9.363 1.00 18.82 ATOM 86 CA LEU 77 48.195 21.810 8.021 1.00 19.38 ATOM 87 CB LEU 77 47.438 23.142 7.864 1.00 19.61 ATOM 88 CG LEU 77 46.056 23.261 7.195 1.00 17.45 ATOM 89 CD1 LEU 77 45.474 24.653 7.434 1.00 13.22 ATOM 90 CD2 LEU 77 46.148 22.973 5.711 1.00 11.85 ATOM 91 C LEU 77 49.680 22.050 7.762 1.00 23.62 ATOM 92 O LEU 77 50.181 21.881 6.642 1.00 28.58 ATOM 93 N GLY 78 50.378 22.474 8.802 1.00 21.75 ATOM 94 CA GLY 78 51.792 22.711 8.676 1.00 21.63 ATOM 95 C GLY 78 52.564 21.405 8.563 1.00 25.33 ATOM 96 O GLY 78 53.384 21.263 7.665 1.00 28.22 ATOM 97 N VAL 79 52.287 20.443 9.449 1.00 24.06 ATOM 98 CA VAL 79 52.998 19.164 9.452 1.00 18.58 ATOM 99 CB VAL 79 52.551 18.244 10.651 1.00 16.10 ATOM 100 CG1 VAL 79 51.241 17.506 10.369 1.00 10.60 ATOM 101 CG2 VAL 79 53.637 17.275 10.986 1.00 9.60 ATOM 102 C VAL 79 52.856 18.464 8.100 1.00 22.38 ATOM 103 O VAL 79 53.835 17.989 7.512 1.00 24.19 ATOM 104 N VAL 80 51.649 18.516 7.563 1.00 19.05 ATOM 105 CA VAL 80 51.330 17.917 6.289 1.00 19.02 ATOM 106 CB VAL 80 49.817 18.051 6.073 1.00 16.18 ATOM 107 CG1 VAL 80 49.453 18.035 4.624 1.00 25.56 ATOM 108 CB2 VAL 80 49.123 16.931 6.820 1.00 14.84 ATOM 109 C VAL 80 52.172 18.488 5.140 1.00 16.87 ATOM 110 O VAL 80 52.399 17.827 4.140 1.00 20.45 ATOM 111 N GLY 81 52.668 19.704 5.319 1.00 16.74 ATOM 112 CA GLY 81 53.499 20.337 4.318 1.00 11.13 ATOM 113 C GLY 81 54.941 19.919 4.468 1.00 13.55 ATOM 114 O GLY 81 55.812 20.383 3.738 1.00 16.53 ATOM 115 N VAL 82 55.200 19.022 5.409 1.00 15.12 ATOM 116 CA VAL 82 56.556 18.526 5.665 1.00 16.31 ATOM 117 CB VAL 82 56.861 18.482 7.176 1.00 14.93 ATOM 118 CG1 VAL 82 58.245 17.911 7.438 1.00 14.94 ATOM 119 CG2 VAL 82 56.758 19.879 7.759 1.00 15.19 ATOM 120 C VAL 82 56.632 17.125 5.094 1.00 14.65 ATOM 121 O VAL 82 55.702 16.348 5.232 1.00 15.48 ATOM 122 N PRO 83 57.754 16.762 4.481 1.00 19.00 ATOM 123 CD PRO 83 58.996 17.501 4.237 1.00 18.29 ATOM 124 CA PRO 83 57.845 15.418 3.917 1.00 22.61 ATOM 125 CB PRO 83 59.296 15.336 3.482 1.00 18.37 ATOM 126 CG PRO 83 59.574 16.726 3.089 1.00 21.28 ATOM 127 C PRO 83 57.526 14.372 4.953 1.00 24.83 ATOM 128 O PRO 83 57.892 14.532 6.124 1.00 29.53 ATOM 129 N PHE 84 56.815 13.335 4.521 1.00 24.14 ATOM 130 CA PHE 84 56.430 12.238 5.382 1.00 25.82 ATOM 131 CB PHE 84 57.675 11.577 5.954 1.00 28.96 ATOM 132 CG PHE 84 58.498 10.908 4.926 1.00 34.74 ATOM 133 CD1 PHE 84 59.878 11.046 4.924 1.00 39.61 ATOM 134 CD2 PHE 84 57.890 10.147 3.937 1.00 35.01 ATOM 135 CE1 PHE 84 60.645 10.431 3.946 1.00 40.72 ATOM 136 CE2 PHE 84 58.638 9.534 2.967 1.00 38.56 ATOM 137 CZ PHE 84 60.023 9.673 2.964 1.00 40.66 ATOM 138 C PHE 84 55.520 12.692 6.493 1.00 27.58 ATOM 139 O PHE 84 55.566 12.154 7.595 1.00 27.77 ATOM 140 N ALA 85 54.689 13.690 6.204 1.00 29.68 ATOM 141 CA ALA 85 53.764 14.220 7.193 1.00 24.88 ATOM 142 CB ALA 85 52.627 13.226 7.437 1.00 21.36 ATOM 143 C ALA 85 54.515 14.562 8.496 1.00 24.27 ATOM 144 O ALA 85 54.003 14.356 9.596 1.00 23.70 ATOM 145 N GLY 86 55.737 15.081 8.338 1.00 22.37 ATOM 146 CA GLY 86 56.560 15.491 9.465 1.00 20.63 ATOM 147 C GLY 86 57.025 14.410 10.409 1.00 22.40 ATOM 148 O GLY 86 57.475 14.705 11.509 1.00 23.81 ATOM 149 N ALA 87 56.976 13.161 9.965 1.00 24.78 ATOM 150 CA ALA 87 57.383 12.303 10.789 1.00 23.69 ATOM 151 CB ALA 87 57.223 10.728 10.041 1.00 23.32 ATOM 152 C ALA 87 58.789 12.145 11.295 1.00 25.85 ATOM 153 O ALA 87 59.114 11.536 12.300 1.00 28.57 ATOM 154 N LEU 88 59.625 12.932 10.629 1.00 24.24 ATOM 155 CA LEU 88 60.995 13.056 11.087 1.00 27.43 ATOM 156 CB LEU 88 61.980 12.910 9.934 1.00 25.11 ATOM 157 CG LEU 88 61.986 11.535 9.297 1.00 24.44 ATOM 158 CD1 LEU 88 63.143 11.477 8.368 1.00 30.54 ATOM 159 CD2 LEU 88 62.115 10.462 10.333 1.00 24.31 ATOM 160 C LEU 88 61.326 14.315 11.872 1.00 32.71 ATOM 161 O LEU 88 62.508 14.586 12.138 1.00 36.61 ATOM 162 N THR 89 60.305 15.074 12.263 1.00 34.99 ATOM 163 CA THR 89 60.530 16.303 13.017 1.00 31.40 ATOM 164 CB THR 89 59.828 17.505 12.335 1.00 31.27 ATOM 165 OG1 THR 89 58.410 17.351 12.419 1.00 36.54 ATOM 166 CG2 THR 89 60.200 17.572 10.860 1.00 26.51 ATOM 167 C THR 89 60.067 16.114 14.467 1.00 30.59 ATOM 168 O THR 89 59.862 14.984 17.913 1.00 29.02 ATOM 169 N SER 90 59.899 17.206 15.206 1.00 30.64 ATOM 170 CA SER 90 59.474 17.091 16.605 1.00 32.41 ATOM 171 CB SER 90 60.435 17.853 17.517 1.00 34.87 ATOM 172 OG SER 90 60.308 19.248 17.313 1.00 42.94 ATOM 173 C SER 90 58.024 17.513 16.871 1.00 28.38 ATOM 174 O SER 90 57.630 17.790 18.010 1.00 25.58 ATOM 175 N PHE 91 57.235 17.519 15.806 1.00 25.68 ATOM 176 CA PHE 91 55.827 17.856 15.817 1.00 27.47 ATOM 177 CB PHE 91 55.147 17.476 14.535 1.00 26.68 ATOM 178 CG PHE 91 53.635 17.344 14.615 1.00 20.42 ATOM 179 CD1 PHE 91 52.825 18.740 14.693 1.00 21.17 ATOM 180 CD2 PHE 91 53.035 16.085 14.615 1.00 21.20 ATOM 181 CE1 PHE 91 51.454 18.351 14.766 1.00 24.02 ATOM 182 CE2 PHE 91 51.665 15.953 14.689 1.00 21.82 ATOM 183 CZ PHE 91 50.867 17.089 14.764 1.00 23.87 ATOM 184 C PHE 91 55.101 17.187 17.050 1.00 28.20 ATOM 185 O PHE 91 54.310 17.841 17.735 1.00 36.57 ATOM 186 N TYR 92 55.375 15.913 17.320 1.00 27.08 ATOM 187 CA TYR 92 54.681 15.220 18.406 1.00 25.16 ATOM 188 CB TYR 92 55.192 13.800 18.545 1.00 25.42 ATOM 189 CG TYR 92 54.629 12.844 17.543 1.00 21.49 ATOM 190 CD1 TYR 92 55.357 11.734 17.146 1.00 24.41 ATOM 191 CE1 TYR 92 54.850 10.833 16.227 1.00 23.54 ATOM 192 CD2 TYR 92 53.370 13.038 16.992 1.00 24.88 ATOM 193 CE2 TYR 92 52.851 12.136 16.060 1.00 22.72 ATOM 194 CZ TYR 92 53.598 11.034 15.688 1.00 22.21 ATOM 195 OH TYR 92 53.085 10.100 14.810 1.00 19.19 ATOM 196 C TYR 92 54.686 15.906 19.763 1.00 25.24 ATOM 197 O TYR 92 53.754 15.738 20.539 1.00 22.91 ATOM 198 N GLN 93 55.725 16.684 20.039 1.00 27.18 ATOM 199 CA GLN 93 55.842 17.399 21.303 1.00 30.97 ATOM 200 CB GLN 93 57.202 18.081 21.397 1.00 39.48 ATOM 201 CG GLN 93 58.371 17.110 21.318 1.00 51.60 ATOM 202 CD GLN 93 58.464 16.206 22.541 1.00 58.73 ATOM 203 OE1 GLN 93 58.420 14.987 22.430 1.00 63.86 ATOM 204 NE2 GLN 93 58.593 16.814 23.716 1.00 61.76 ATOM 205 C GLN 93 54.744 18.441 21.430 1.00 31.82 ATOM 206 O GLN 93 54.101 18.539 22.481 1.00 31.42 ATOM 207 N SER 94 54.535 19.215 20.361 1.00 31.11 ATOM 208 CA SER 94 53.498 20.244 20.341 1.00 29.17 ATOM 209 CB SER 94 53.567 21.108 19.082 1.00 27.65 ATOM 210 OG SER 94 54.701 21.944 19.083 1.00 36.29 ATOM 211 C SER 94 52.153 19.563 20.388 1.00 30.39 ATOM 212 O SER 94 51.294 19.937 21.194 1.00 32.51 ATOM 213 N PHE 95 51.985 18.549 19.537 1.00 28.11 ATOM 214 CA PHE 95 50.739 17.791 19.483 1.00 28.46 ATOM 215 CB PHE 95 50.832 16.657 18.454 1.00 27.56 ATOM 216 CG PHE 95 49.502 16.068 18.086 1.00 28.26 ATOM 217 CD1 PHE 95 48.473 16.883 17.610 1.00 24.62 ATOM 218 CD2 PHE 95 49.270 14.703 18.224 1.00 25.73 ATOM 219 CE1 PHE 95 47.234 16.340 17.282 1.00 22.34 ATOM 220 CE2 PHE 95 48.031 14.153 17.895 1.00 22.66 ATOM 221 CZ PHE 95 47.011 14.971 17.424 1.00 18.98 ATOM 222 C PHE 95 50.390 17.241 20.875 1.00 26.55 ATOM 223 O PHE 95 49.230 17.306 21.287 1.00 29.64 ATOM 224 N LEU 96 51.384 16.752 21.617 1.00 26.06 ATOM 225 CA LEU 96 51.133 16.232 22.959 1.00 25.65 ATOM 226 CB LEU 96 52.395 15.670 23.587 1.00 25.73 ATOM 227 CG LEU 96 52.764 14.221 23.325 1.00 28.75 ATOM 228 CD1 LEU 96 53.909 13.824 24.246 1.00 31.30 ATOM 229 CD2 LEU 96 51.583 13.334 23.583 1.00 33.49 ATOM 230 C LEU 96 50.581 17.294 23.895 1.00 25.90 ATOM 231 O LEU 96 49.544 17.079 24.554 1.00 24.48 ATOM 232 N ASN 97 51.240 18.444 23.951 1.00 28.33 ATOM 233 CA ASN 97 50.785 19.512 24.840 1.00 32.74 ATOM 234 CB ASN 97 51.680 20.753 24.740 1.00 36.47 ATOM 235 CG ASN 97 53.154 20.434 24.807 1.00 47.89 ATOM 236 OD1 ASN 97 53.985 21.175 24.248 1.00 53.39 ATOM 237 ND1 ASN 97 53.507 19.351 25.504 1.00 52.31 ATOM 238 C ASN 97 49.355 19.967 24.535 1.00 34.80 ATOM 239 O ASN 97 48.555 20.198 25.444 1.00 38.94 ATOM 240 N THR 98 49.048 20.122 23.254 1.00 31.52 ATOM 241 CA THR 98 47.755 20.608 22.849 1.00 27.60 ATOM 242 CB THR 98 47.855 21.264 21.458 1.00 32.02 ATOM 243 OG1 THR 98 46.576 21.759 21.047 1.00 35.15 ATOM 244 OG2 THR 98 48.389 20.301 20.449 1.00 31.67 ATOM 245 C THR 98 46.597 19.632 22.954 1.00 26.56 ATOM 246 O THR 98 45.568 19.985 23.504 1.00 26.90 ATOM 247 N ILE 99 46.771 18.398 22.495 1.00 25.90 ATOM 248 CA ILE 99 45.694 17.414 22.542 1.00 22.63 ATOM 249 CB ILE 99 45.495 16.771 21.138 1.00 21.44 ATOM 250 CG2 ILE 99 44.567 15.567 21.204 1.00 21.56 ATOM 251 CG1 ILE 99 44.888 17.780 20.176 1.00 18.21 ATOM 252 CD1 ILE 99 43.507 18.260 20.597 1.00 21.58 ATOM 253 C ILE 99 45.823 16.317 23.638 1.00 26.20 ATOM 254 O ILE 99 44.823 15.947 24.283 1.00 19.95 ATOM 255 N TRP 100 47.036 15.824 23.896 1.00 25.49 ATOM 256 CA TRP 100 47.195 14.775 24.907 1.00 29.32 ATOM 257 CB TRP 100 47.826 13.507 24.301 1.00 21.69 ATOM 258 CG TRP 100 47.076 12.975 23.125 1.00 19.06 ATOM 259 CD2 TRP 100 45.988 12.031 23.134 1.00 18.83 ATOM 260 CE2 TRP 100 45.564 11.866 21.798 1.00 14.99 ATOM 261 CE3 TRP 100 45.325 11.316 24.139 1.00 18.15 ATOM 262 CD1 TRP 100 47.262 13.324 21.818 1.00 21.00 ATOM 263 NE1 TRP 100 46.357 12.667 21.018 1.00 19.19 ATOM 264 CZ2 TRP 100 44.517 11.022 21.440 1.00 14.21 ATOM 265 CZ3 TRP 100 44.278 10.471 23.777 1.00 18.67 ATOM 266 CH2 TRP 100 43.886 10.334 22.441 1.00 14.87 ATOM 267 C TRP 100 47.945 15.199 26.176 1.00 31.48 ATOM 268 O TRP 100 48.938 14.585 26.560 1.00 32.21 ATOM 269 N PRO 101 47.465 16.250 26.854 1.00 34.11 ATOM 270 CD PRO 101 46.288 17.090 26.574 1.00 34.77 ATOM 271 CA PRO 101 48.135 16.694 28.074 1.00 38.53 ATOM 272 CB PRO 101 47.586 18.105 28.248 1.00 38.92 ATOM 273 CG PRO 101 46.169 17.937 27.818 1.00 37.10 ATOM 274 C PRO 101 47.713 15.771 29.219 1.00 39.63 ATOM 275 O PRO 101 46.600 15.224 29.192 1.00 39.50 ATOM 276 N SER 102 48.567 15.633 30.235 1.00 41.84 ATOM 277 CA SER 102 48.283 14.754 31.372 1.00 42.97 ATOM 278 CB SER 102 49.412 14.819 32.397 1.00 44.81 ATOM 279 OG SER 102 50.492 13.979 32.036 1.00 48.18 ATOM 280 C SER 102 46.935 14.949 32.072 1.00 46.58 ATOM 281 O SER 102 46.304 13.965 32.470 1.00 47.97 ATOM 282 N ASP 103 46.487 16.199 32.211 1.00 47.92 ATOM 283 CA ASP 103 45.209 16.500 32.872 1.00 48.48 ATOM 284 CB ASP 103 45.213 17.935 33.379 1.00 51.18 ATOM 285 CG ASP 103 45.529 18.936 32.289 1.00 54.93 ATOM 286 OD1 ASP 103 44.942 18.862 31.177 1.00 53.60 ATOM 287 OD2 ASP 103 46.375 19.813 32.558 1.00 61.10 ATOM 288 C ASP 103 43.932 16.268 32.049 1.00 48.05 ATOM 289 O ASP 103 42.835 16.518 32.542 1.00 52.24 ATOM 290 N ALA 104 44.085 15.863 30.788 1.00 45.10 ATOM 291 CA ALA 104 42.941 15.591 29.873 1.00 39.51 ATOM 292 CB ALA 104 42.393 14.204 30.114 1.00 40.01 ATOM 293 C ALA 104 41.863 16.630 29.850 1.00 39.09 ATOM 294 O ALA 104 40.698 16.314 29.606 1.00 34.52 ATOM 295 N ASP 105 42.235 17.881 30.074 1.00 38.82 ATOM 296 CA ASP 105 41.266 18.964 30.028 1.00 39.02 ATOM 297 CB ASP 105 41.930 20.288 30.370 1.00 43.59 ATOM 298 CG ASP 105 42.173 20.445 31.846 1.00 52.33 ATOM 299 OD1 ASP 105 43.073 21.242 32.199 1.00 57.65 ATOM 300 OD2 ASP 105 41.465 19.781 32.650 1.00 54.73 ATOM 301 C ASP 105 40.613 19.072 28.657 1.00 34.78 ATOM 302 O ASP 105 39.385 19.155 28.551 1.00 35.07 ATOM 303 N PRO 106 41.423 19.017 27.582 1.00 30.97 ATOM 304 CD PRO 106 42.876 18.735 27.539 1.00 27.68 ATOM 305 CA PRO 106 40.882 19.116 26.226 1.00 27.20 ATOM 306 CB PRO 106 42.044 18.617 25.371 1.00 26.38 ATOM 307 CG PRO 106 43.232 19.059 26.125 1.00 27.63 ATOM 308 C PRO 106 39.639 18.259 25.990 1.00 25.44 ATOM 309 O PRO 106 38.660 18.711 25.416 1.00 32.50 ATOM 310 N TRP 107 39.684 17.025 26.457 1.00 22.67 ATOM 311 CA TRP 107 38.604 16.080 26.270 1.00 21.40 ATOM 312 CB TRP 107 39.090 14.697 26.695 1.00 21.20 ATOM 313 CG TRP 107 40.377 14.367 26.011 1.00 21.35 ATOM 314 CD2 TRP 107 40.549 14.025 24.630 1.00 23.47 ATOM 315 CE2 TRP 107 41.926 13.818 24.418 1.00 26.19 ATOM 316 CE3 TRP 107 39.666 13.859 23.552 1.00 22.11 ATOM 317 CD1 TRP 107 41.617 14.367 26.558 1.00 22.90 ATOM 318 NE1 TRP 107 42.560 14.040 25.610 1.00 23.51 ATOM 319 CZ2 TRP 107 42.442 13.453 23.171 1.00 27.67 ATOM 320 CZ3 TRP 107 40.175 13.499 22.326 1.00 14.25 ATOM 321 CH2 TRP 107 41.551 13.294 22.144 1.00 23.37 ATOM 322 C TRP 107 37.305 16.463 26.944 1.00 22.55 ATOM 323 O TRP 107 36.249 16.431 26.323 1.00 17.29 ATOM 324 N LYS 108 37.375 16.879 28.200 1.00 28.78 ATOM 325 CA LYS 108 36.156 17.274 28.902 1.00 31.84 ATOM 326 CB LYS 108 36.463 17.711 30.334 1.00 33.26 ATOM 327 CG LYS 108 37.016 16.622 31.215 1.00 38.45 ATOM 328 CD LYS 108 38.128 17.191 32.086 1.00 48.94 ATOM 329 CE LYS 108 38.924 16.104 32.803 1.00 54.01 ATOM 330 NZ LYS 108 40.202 16.621 33.392 1.00 55.46 ATOM 331 C LYS 108 35.513 18.416 28.120 1.00 30.68 ATOM 332 O LYS 108 34.296 18.572 28.130 1.00 35.50 ATOM 333 N ALA 109 36.342 19.190 27.428 1.00 28.04 ATOM 334 CA ALA 109 35.885 20.306 26.609 1.00 27.59 ATOM 335 CB ALA 109 37.064 21.153 26.194 1.00 33.31 ATOM 336 C ALA 109 35.144 19.817 25.372 1.00 26.82 ATOM 337 O ALA 109 34.100 20.362 24.999 1.00 28.89 ATOM 338 N PHE 110 35.688 18.796 24.723 1.00 23.59 ATOM 339 CA PHE 110 35.043 18.245 23.548 1.00 21.61 ATOM 340 CB PHE 110 35.998 17.325 22.801 1.00 22.67 ATOM 341 CG PHE 110 37.166 18.041 22.180 1.00 24.76 ATOM 342 CD1 PHE 110 38.474 17.607 22.421 1.00 22.40 ATOM 343 CD2 PHE 110 36.960 19.151 21.361 1.00 19.11 ATOM 344 CE1 PHE 110 39.555 18.274 21.859 1.00 25.16 ATOM 345 CE2 PHE 110 38.033 19.818 20.796 1.00 24.29 ATOM 346 CZ PHE 110 39.334 19.383 21.044 1.00 24.30 ATOM 347 C PHE 110 33.791 17.482 23.965 1.00 35.43 ATOM 348 O PHE 110 32.754 17.566 23.304 1.00 26.45 ATOM 349 N MET 111 33.883 16.801 25.109 1.00 29.94 ATOM 350 CA MET 111 32.788 16.020 25.687 1.00 30.42 ATOM 351 CB MET 111 33.255 15.316 26.957 1.00 28.69 ATOM 352 CG MET 111 34.336 14.297 26.747 1.00 32.84 ATOM 353 SD MET 111 33.729 12.637 26.927 1.00 32.93 ATOM 354 CE MET 111 35.263 11.745 26.874 1.00 35.32 ATOM 355 C MET 111 31.591 16.886 26.058 1.00 31.28 ATOM 356 O MET 111 30.478 16.375 26.195 1.00 35.76 ATOM 357 N ALA 112 31.821 18.180 26.276 1.00 33.59 ATOM 358 CA ALA 112 30.737 19.103 26.650 1.00 36.25 ATOM 359 CB ALA 112 31.117 19.895 27.908 1.00 37.41 ATOM 360 C ALA 112 30.348 20.073 25.536 1.00 35.59 ATOM 361 O ALA 112 29.274 20.690 25.578 1.00 36.38 ATOM 362 N GLN 113 31.192 30.153 24.517 1.00 29.50 ATOM 363 CA GLN 113 30.958 21.070 23.438 1.00 25.32 ATOM 364 CB GLN 113 32.137 21.034 22.459 1.00 28.47 ATOM 365 CG GLN 113 31.821 21.592 21.091 1.00 22.47 ATOM 366 CD GLN 113 33.006 21.581 20.152 1.00 22.91 ATOM 367 OE1 GLN 113 33.272 22.581 19.471 1.00 18.94 ATOM 368 NE2 GLN 113 33.722 20.450 20.091 1.00 16.92 ATOM 369 C GLN 113 29.659 20.830 22.714 1.00 23.43 ATOM 370 O GLN 113 28.956 21.770 22.387 1.00 24.46 ATOM 371 N VAL 114 29.306 19.583 22.472 1.00 23.56 ATOM 372 CA VAL 114 28.091 19.362 21.721 1.00 22.74 ATOM 373 CB VAL 114 28.206 18.138 20.835 1.00 24.34 ATOM 374 CG1 VAL 114 27.267 18.280 19.657 1.00 24.59 ATOM 375 CG2 VAL 114 29.630 17.968 20.349 1.00 18.65 ATOM 376 C VAL 114 26.818 19.322 22.563 1.00 26.29 ATOM 377 O VAL 114 25.756 19.710 22.083 1.00 27.22 ATOM 378 N GLU 115 26.927 18.897 23.820 1.00 26.49 ATOM 379 CA GLU 115 25.778 18.857 24.719 1.00 23.95 ATOM 380 CB GLU 115 26.230 18.527 26.148 1.00 26.34 ATOM 381 CG GLU 115 26.726 17.072 26.345 1.00 27.76 ATOM 382 CD GLU 115 27.170 16.764 27.780 1.00 34.27 ATOM 383 OE1 GLU 115 27.688 17.665 28.494 1.00 34.36 ATOM 384 OE2 GLU 115 27.005 15.604 28.200 1.00 34.20 ATOM 385 C GLU 115 25.170 20.250 24.665 1.00 24.85 ATOM 386 O GLU 115 23.971 20.405 24.453 1.00 26.55 ATOM 387 N VAL 116 26.041 21.254 24.740 1.00 23.84 ATOM 388 CA VAL 116 25.675 22.675 24.680 1.00 26.40 ATOM 389 CB VAL 116 26.963 23.573 24.910 1.00 26.32 ATOM 390 CG1 VAL 116 26.732 25.017 24.498 1.00 22.18 ATOM 391 CG2 VAL 116 27.417 23.519 26.378 1.00 22.96 ATOM 392 C VAL 116 24.982 23.087 23.354 1.00 31.33 ATOM 393 O VAL 116 24.060 23.912 23.357 1.00 30.41 ATOM 394 N LEU 117 25.428 22.516 22.233 1.00 34.23 ATOM 395 CA LEU 117 24.884 22.852 20.912 1.00 33.73 ATOM 396 CB LEU 117 25.917 22.601 19.801 1.00 28.04 ATOM 397 CG LEU 117 27.208 23.430 19.781 1.00 29.91 ATOM 398 CD1 LEU 117 28.256 22.795 18.853 1.00 24.06 ATOM 399 CD2 LEU 117 26.906 24.848 19.368 1.00 25.56 ATOM 400 C LEU 117 23.585 22.144 20.568 1.00 35.30 ATOM 401 O LEU 117 22.852 22.593 19.692 1.00 41.08 ATOM 402 N ILE 118 23.315 20.998 21.171 1.00 32.43 ATOM 403 CA ILE 118 22.056 20.350 20.861 1.00 34.23 ATOM 404 CB ILE 118 22.219 18.996 20.103 1.00 33.52 ATOM 405 CG2 ILE 118 22.754 19.223 18.688 1.00 34.50 ATOM 406 CG1 ILE 118 23.104 18.030 20.880 1.00 31.03 ATOM 407 CD1 ILE 118 23.022 16.619 20.353 1.00 28.15 ATOM 408 C ILE 118 21.268 20.161 22.140 1.00 36.68 ATOM 409 O ILE 118 20.284 19.420 22.174 1.00 40.44 ATOM 410 N ASP 119 21.668 20.898 23.173 1.00 42.31 ATOM 411 CA ASP 119 21.037 20.819 24.487 1.00 48.51 ATOM 412 CB ASP 119 19.998 21.936 24.690 1.00 53.59 ATOM 413 CG ASP 119 20.619 23.201 25.331 1.00 63.54 ATOM 414 OD1 ASP 119 20.738 23.251 26.582 1.00 67.03 ATOM 415 OD2 ASP 119 21.023 24.133 24.588 1.00 66.97 ATOM 416 C ASP 119 20.515 19.416 24.824 1.00 47.46 ATOM 417 O ASP 119 19.316 19.175 25.000 1.00 46.57 ATOM 418 N LYS 120 21.474 18.499 24.884 1.00 45.37 ATOM 419 CA LYS 120 21.247 17.099 25.180 1.00 43.83 ATOM 420 CB LYS 120 21.220 16.296 23.874 1.00 48.35 ATOM 421 CG LYS 120 20.134 15.228 23.781 1.00 54.30 ATOM 422 CD LYS 120 20.675 14.015 23.024 1.00 64.38 ATOM 423 CE LYS 120 19.703 12.838 22.981 1.00 66.37 ATOM 424 NZ LYS 120 20.427 11.562 22.663 1.00 65.78 ATOM 425 C LYS 120 22.465 16.724 26.022 1.00 40.72 ATOM 426 O LYS 120 23.413 17.504 26.103 1.00 36.78 ATOM 427 N LYS 121 22.446 15.552 26.650 1.00 40.87 ATOM 428 CA LYS 121 23.558 15.121 27.499 1.00 44.88 ATOM 429 CB LYS 121 23.203 15.298 28.984 1.00 52.11 ATOM 430 CG LYS 121 22.708 16.683 29.408 1.00 62.07 ATOM 431 CD LYS 121 23.801 17.739 29.350 1.00 69.11 ATOM 432 CE LYS 121 23.201 19.140 29.325 1.00 73.00 ATOM 433 NZ LYS 121 24.267 20.155 29.145 1.00 75.31 ATOM 434 C LYS 121 23.918 13.656 27.293 1.00 42.40 ATOM 435 O LYS 121 23.043 12.839 26.977 1.00 40.70 ATOM 436 N ILE 122 25.207 13.344 27.464 1.00 39.16 ATOM 437 CA ILE 122 25.722 11.972 27.363 1.00 38.99 ATOM 438 CB ILE 122 27.239 11.901 27.043 1.00 36.73 ATOM 439 CG2 ILE 122 27.612 10.470 26.694 1.00 33.96 ATOM 440 CG1 ILE 122 27.617 12.828 25.893 1.00 34.62 ATOM 441 CD1 ILE 122 29.092 13.137 25.858 1.00 27.87 ATOM 442 C ILE 122 35.575 11.413 28.777 1.00 39.57 ATOM 443 O ILE 122 26.043 12.018 29.743 1.00 39.64 ATOM 444 N GLU 123 24.978 10.245 28.921 1.00 40.10 ATOM 445 CA GLU 123 24.814 9.750 30.259 1.00 44.03 ATOM 446 CB GLU 123 23.874 8.566 30.281 1.00 49.74 ATOM 447 CG GLU 123 22.459 8.971 29.925 1.00 60.66 ATOM 448 CD GLU 123 21.423 7.983 30.411 1.00 71.25 ATOM 449 OE1 GLU 123 21.199 6.953 29.724 1.00 75.21 ATOM 450 OE2 GLU 123 20.830 8.246 31.486 1.00 77.91 ATOM 451 C GLU 123 26.138 9.462 30.922 1.00 45.02 ATOM 452 O GLU 123 27.136 9.236 30.249 1.00 46.99 ATOM 453 N GLU 124 26.143 9.520 32.248 1.00 45.66 ATOM 454 CA GLU 124 27.336 9.291 33.050 1.00 46.67 ATOM 455 CB GLU 124 26.985 9.301 34.547 1.00 58.31 ATOM 456 CG GLU 124 26.307 8.014 35.136 1.00 79.38 ATOM 457 CD GLU 124 24.862 7.728 34.639 1.00 88.11 ATOM 458 OE1 GLU 124 24.036 8.669 34.506 1.00 93.57 ATOM 459 OE2 GLU 124 24.545 6.535 34.414 1.00 92.35 ATOM 460 C GLU 124 28.184 8.059 32.716 1.00 43.44 ATOM 461 O GLU 124 29.398 8.182 32.541 1.00 41.19 ATOM 462 N TYR 125 27.564 6.882 32.624 1.00 39.19 ATOM 463 CA TYR 125 28.305 5.654 32.342 1.00 38.90 ATOM 464 CB TYR 125 27.362 4.460 32.153 1.00 41.22 ATOM 465 CG TYR 125 26.336 4.629 31.048 1.00 52.24 ATOM 466 CD1 TYR 125 26.540 4.059 29.789 1.00 57.21 ATOM 467 CE1 TYR 125 25.616 4.229 28.750 1.00 62.24 ATOM 468 CD2 TYR 125 25.169 5.373 31.251 1.00 54.99 ATOM 469 CE2 TYR 125 24.236 5.548 30.224 1.00 60.71 ATOM 470 CZ TYR 125 24.464 4.976 28.970 1.00 65.04 ATOM 471 OH TYR 125 23.562 5.164 27.932 1.00 65.65 ATOM 472 C TYR 125 29.176 5.833 31.120 1.00 38.81 ATOM 473 O TYR 125 30.398 5.774 31.198 1.00 39.40 ATOM 474 N ALA 126 28.529 6.200 30.025 1.00 38.18 ATOM 475 CA ALA 126 29.189 6.395 28.759 1.00 35.81 ATOM 476 CB ALA 126 28.160 6.777 27.715 1.00 36.47 ATOM 477 C ALA 126 30.300 7.438 28.836 1.00 35.33 ATOM 478 O ALA 126 31.416 7.184 28.390 1.00 39.00 ATOM 479 N LYS 127 30.015 8.575 29.457 1.00 33.83 ATOM 480 CA LYS 127 30.979 9.666 29.580 1.00 36.03 ATOM 481 CB LYS 127 30.264 10.897 30.143 1.00 37.06 ATOM 482 CG LYS 127 30.934 12.227 29.859 1.00 44.50 ATOM 483 CD LYS 127 29.936 13.399 30.033 1.00 50.75 ATOM 484 CE LYS 127 30.562 14.783 29.762 1.00 49.31 ATOM 485 NZ LYS 127 29.576 15.897 29.940 1.00 48.12 ATOM 486 C LYS 127 32.235 9.330 30.412 1.00 38.28 ATOM 487 O LYS 127 33.350 9.752 30.084 1.00 39.37 ATOM 488 N SER 128 32.086 8.557 31.479 1.00 38.74 ATOM 489 CA SER 128 33.262 8.242 32.281 1.00 40.98 ATOM 490 CB SER 128 32.863 7.861 33.705 1.00 43.21 ATOM 491 OG SER 128 31.778 6.953 33.707 1.00 54.17 ATOM 492 C SER 128 34.102 7.155 31.621 1.00 39.36 ATOM 493 O SER 128 35.335 7.178 31.674 1.00 38.65 ATOM 494 N LYS 129 33.421 6.238 30.946 1.00 37.47 ATOM 495 CA LYS 129 34.081 5.145 30.254 1.00 35.27 ATOM 496 CB LYS 129 33.027 4.216 29.643 1.00 37.51 ATOM 497 CG LYS 129 33.446 2.768 29.510 1.00 41.85 ATOM 498 CD LYS 129 34.432 2.565 28.374 1.00 51.04 ATOM 499 CE LYS 129 35.429 1.457 28.704 1.00 55.30 ATOM 500 NZ LYS 129 36.243 1.784 29.934 1.00 58.49 ATOM 501 C LYS 129 34.967 5.782 29.186 1.00 33.07 ATOM 502 O LYS 129 36.155 5.469 29.070 1.00 33.07 ATOM 503 N ALA 130 34.415 6.740 28.460 1.00 29.50 ATOM 504 CA ALA 130 35.192 7.414 27.438 1.00 26.51 ATOM 505 CB ALA 130 34.335 8.429 26.699 1.00 27.54 ATOM 506 C ALA 130 36.425 8.081 28.055 1.00 25.32 ATOM 507 O ALA 130 37.531 7.871 27.566 1.00 29.93 ATOM 508 N LEU 131 36.262 8.868 29.119 1.00 21.01 ATOM 509 CA LEU 131 37.420 9.508 29.745 1.00 18.71 ATOM 510 CB LEU 131 36.993 10.317 30.944 1.00 19.17 ATOM 511 CG LEU 131 36.275 11.598 30.568 1.00 28.02 ATOM 512 CD1 LEU 131 35.753 12.262 31.826 1.00 32.84 ATOM 513 CD2 LEU 131 37.217 12.538 29.844 1.00 26.14 ATOM 514 C LEU 131 38.480 8.503 30.189 1.00 21.44 ATOM 515 O LEU 131 39.676 8.813 30.234 1.00 22.24 ATOM 516 N ALA 132 38.030 7.311 30.557 1.00 22.62 ATOM 517 CA ALA 132 38.917 6.236 30.997 1.00 27.46 ATOM 518 CB ALA 132 38.089 5.090 31.584 1.00 24.97 ATOM 519 C ALA 132 39.780 5.720 29.838 1.00 28.21 ATOM 520 O ALA 132 41.021 5.616 29.962 1.00 28.54 ATOM 521 N GLU 133 39.113 5.395 28.725 1.00 24.88 ATOM 522 CA GLU 133 37.788 4.906 27.534 1.00 21.77 ATOM 523 CB GLU 133 38.806 4.655 26.394 1.00 20.10 ATOM 524 CG GLU 133 37.982 3.382 26.535 1.00 22.13 ATOM 525 CD GLU 133 38.836 2.133 26.735 1.00 29.26 ATOM 526 OE1 GLU 133 39.035 1.721 27.897 1.00 32.94 ATOM 527 OE2 GLU 133 39.303 1.555 35.733 1.00 33.24 ATOM 528 C GLU 133 40.798 5.938 27.135 1.00 22.44 ATOM 529 O GLU 133 41.963 5.613 26.908 1.00 25.37 ATOM 530 N LEU 134 40.367 7.198 27.137 1.00 25.68 ATOM 531 CA LEU 134 41.237 8.330 26.794 1.00 27.08 ATOM 532 CB LEU 134 40.439 9.650 26.759 1.00 25.70 ATOM 533 CG LEU 134 39.500 9.925 25.573 1.00 24.82 ATOM 534 CD1 LEU 134 38.672 11.152 25.847 1.00 26.04 ATOM 535 CD2 LEU 134 40.285 10.101 24.281 1.00 23.46 ATOM 536 C LEU 134 42.452 8.459 27.732 1.00 28.99 ATOM 537 O LEU 134 43.526 8.874 27.296 1.00 31.43 ATOM 538 N GLN 135 42.298 8.100 29.007 1.00 29.30 ATOM 539 CA GLN 135 43.416 8.184 29.933 1.00 24.79 ATOM 540 CB GLN 135 42.984 7.936 31.359 1.00 37.17 ATOM 541 CG GLN 135 44.183 7.664 32.243 1.00 50.15 ATOM 542 CD GLN 135 43.898 7.810 33.710 1.00 57.04 ATOM 543 OE1 GLN 135 44.561 8.593 34.395 1.00 60.77 ATOM 544 NE2 GLN 135 42.938 7.036 34.218 1.00 62.19 ATOM 545 C GLN 135 44.445 7.154 29.565 1.00 19.79 ATOM 546 O GLN 135 45.643 7.431 29.595 1.00 19.13 ATOM 547 N GLY 136 43.983 5.944 29.286 1.00 18.03 ATOM 548 CA GLY 136 44.901 4.890 28.879 1.00 21.15 ATOM 549 C GLY 136 45.595 5.199 27.543 1.00 21.95 ATOM 550 O GLY 136 46.760 4.862 27.338 1.00 20.39 ATOM 551 N LEU 137 44.887 5.863 26.636 1.00 17.33 ATOM 552 CA LEU 137 45.450 6.204 25.348 1.00 17.93 ATOM 553 CB LEU 137 44.346 6.640 24.382 1.00 20.38 ATOM 554 CG LEU 137 43.472 5.486 23.897 1.00 17.15 ATOM 555 CD1 LEU 137 42.219 5.983 23.217 1.00 22.09 ATOM 556 CD2 LEU 137 44.292 4.635 22.970 1.00 19.05 ATOM 557 C LEU 137 46.527 7.259 25.439 1.00 18.12 ATOM 558 O LEU 137 47.564 7.143 24.799 1.00 20.83 ATOM 559 N GLN 138 46.294 8.293 26.231 1.00 19.01 ATOM 560 CA GLN 138 47.274 9.364 26.373 1.00 23.17 ATOM 561 CB GLN 138 46.756 10.428 27.354 1.00 29.42 ATOM 562 CG GLN 138 47.680 11.615 27.608 1.00 33.61 ATOM 563 CD GLN 138 48.671 11.359 28.736 1.00 38.81 ATOM 564 OE1 GLN 138 49.881 11.383 28.525 1.00 43.59 ATOM 565 NE2 GLN 138 48.161 11.112 29.938 1.00 40.08 ATOM 566 C GLN 138 48.581 8.777 26.854 1.00 24.66 ATOM 567 O GLN 138 49.654 9.111 26.359 1.00 26.00 ATOM 568 N ASN 139 48.464 7.858 27.796 1.00 24.89 ATOM 569 CA ASN 139 49.614 7.203 28.376 1.00 26.38 ATOM 570 CB ASN 139 49.127 6.275 29.474 1.00 28.88 ATOM 571 CG ASN 139 50.211 5.915 30.436 1.00 33.91 ATOM 572 OD1 ASN 139 50.747 4.798 30.407 1.00 29.67 ATOM 573 ND2 ASN 139 50.554 6.863 31.305 1.00 34.35 ATOM 574 C ASN 139 50.432 6.422 27.328 1.00 29.07 ATOM 575 O ASN 139 51.619 6.706 27.106 1.00 30.84 ATOM 576 N ASN 140 49.788 5.453 26.674 1.00 27.61 ATOM 577 CA ASN 140 50.425 4.631 25.647 1.00 26.41 ATOM 578 CB ASN 140 49.382 3.763 24.947 1.00 28.07 ATOM 579 CG ASN 140 49.055 2.524 25.706 1.00 26.17 ATOM 580 OD1 ASN 140 47.969 1.982 25.586 1.00 33.30 ATOM 581 ND2 ASN 140 50.001 2.042 26.471 1.00 34.68 ATOM 582 C ASN 140 51.102 5.492 24.594 1.00 30.46 ATOM 583 O ASN 140 52.269 5.266 24.217 1.00 31.28 ATOM 584 N PHE 141 50.332 6.462 24.106 1.00 30.47 ATOM 585 CA PHE 141 50.777 7.375 23.083 1.00 26.60 ATOM 586 CB PHE 141 49.643 8.294 22.656 1.00 23.65 ATOM 587 CG PHE 141 50.001 9.127 21.500 1.00 23.59 ATOM 588 CD1 PHE 141 50.354 8.532 20.302 1.00 19.79 ATOM 589 CD2 PHE 141 50.123 10.503 21.631 1.00 25.06 ATOM 590 CE1 PHE 141 50.840 9.269 19.254 1.00 21.84 ATOM 591 CE2 PHE 141 50.612 11.264 20.582 1.00 22.29 ATOM 592 CZ PHE 141 50.974 10.640 19.391 1.00 18.99 ATOM 593 C PHE 141 51.970 8.192 23.519 1.00 26.32 ATOM 594 O PHE 141 52.962 8.285 22.790 1.00 28.72 ATOM 595 N GLU 142 51.900 8.774 24.710 1.00 26.35 ATOM 596 CA GLU 142 53.025 9.568 25.197 1.00 26.18 ATOM 597 CB GLU 142 52.657 10.297 26.484 1.00 26.40 ATOM 598 CG GLU 142 53.828 11.060 27.085 1.00 34.98 ATOM 599 CD GLU 142 53.429 12.038 28.189 1.00 38.85 ATOM 600 OE1 GLU 142 52.358 11.876 28.826 1.00 40.50 ATOM 601 OE2 GLU 142 54.209 12.985 28.417 1.00 41.79 ATOM 602 C GLU 142 54.265 8.680 25.387 1.00 25.06 ATOM 603 O GLU 142 55.394 9.097 25.125 1.00 26.60 ATOM 604 N ASP 143 54.045 7.451 25.836 1.00 25.61 ATOM 605 CA ASP 143 55.118 6.494 26.029 1.00 22.86 ATOM 606 CB ASP 143 54.521 5.161 26.422 1.00 29.76 ATOM 607 CG ASP 143 54.827 4.793 27.835 1.00 32.84 ATOM 608 OD1 ASP 143 55.385 5.646 28.546 1.00 35.88 ATOM 609 OD2 ASP 143 54.524 3.647 28.236 1.00 38.26 ATOM 610 C ASP 143 55.820 6.341 24.704 1.00 24.52 ATOM 611 O ASP 143 57.009 6.642 24.576 1.00 28.26 ATOM 612 N TYR 144 55.039 5.970 23.693 1.00 22.82 ATOM 613 CA TYR 144 55.536 5.783 22.346 1.00 17.47 ATOM 614 CB TYR 144 54.379 5.515 21.384 1.00 18.87 ATOM 615 CG TYR 144 54.755 5.589 19.914 1.00 20.91 ATOM 616 CD1 TYR 144 55.499 4.573 19.303 1.00 24.91 ATOM 617 CE1 TYR 144 55.859 4.653 17.944 1.00 17.76 ATOM 618 CD2 TYR 144 54.376 6.685 19.128 1.00 26.29 ATOM 619 CE2 TYR 144 54.730 6.764 17.770 1.00 19.32 ATOM 620 CZ TYR 144 55.470 5.746 17.200 1.00 16.89 ATOM 621 OH TYR 144 55.844 5.836 15.895 1.00 19.87 ATOM 622 C TYR 144 56.330 6.977 21.865 1.00 17.93 ATOM 623 O TYR 144 57.437 6.822 21.371 1.00 17.85 ATOM 624 N VAL 145 55.776 8.173 21.987 1.00 17.19 ATOM 625 CA VAL 145 56.507 9.328 21.509 1.00 15.32 ATOM 626 CB VAL 145 55.734 10.599 21.731 1.00 15.48 ATOM 627 CG1 VAL 145 56.622 11.814 21.404 1.00 13.94 ATOM 628 CG2 VAL 145 54.487 10.570 20.850 1.00 9.58 ATOM 629 C VAL 145 57.896 9.437 22.110 1.00 20.37 ATOM 630 O VAL 145 58.856 9.754 21.405 1.00 21.53 ATOM 631 N ASN 146 58.011 9.115 23.397 1.00 19.99 ATOM 632 CA ASN 146 59.297 9.165 24.082 1.00 22.23 ATOM 633 CB ASN 146 59.138 9.071 25.592 1.00 26.65 ATOM 634 CG ASN 146 58.687 10.375 26.192 1.00 23.52 ATOM 635 OD1 ASN 146 58.612 11.393 25.506 1.00 32.61 ATOM 636 ND2 ASN 146 58.371 10.356 27.461 1.00 33.71 ATOM 637 C ASN 146 60.239 8.117 23.584 1.00 18.20 ATOM 638 O ASN 146 61.409 8.405 23.380 1.00 21.90 ATOM 639 N ALA 147 59.743 6.902 23.393 1.00 17.72 ATOM 640 CA ALA 147 60.559 5.823 22.839 1.00 17.53 ATOM 641 CB ALA 147 59.754 4.519 22.779 1.00 17.05 ATOM 642 C ALA 147 60.970 6.222 21.417 1.00 22.69 ATOM 643 O ALA 147 62.035 7.026 20.752 1.00 27.83 ATOM 644 N LEU 148 60.142 7.026 20.752 1.00 24.44 ATOM 645 CA LEU 148 60.442 7.423 19.388 1.00 25.40 ATOM 646 CB LEU 148 59.180 7.831 18.619 1.00 22.84 ATOM 647 CG LEU 148 59.406 8.092 17.125 1.00 22.68 ATOM 648 CD1 LEU 148 59.589 6.805 16.322 1.00 18.18 ATOM 649 CD2 LEU 148 58.268 8.886 16.582 1.00 20.06 ATOM 650 C LEU 148 61.480 8.508 19.308 1.00 24.34 ATOM 651 O LEU 148 62.312 8.462 18.435 1.00 27.64 ATOM 652 N ASN 149 61.474 9.465 20.222 1.00 28.78 ATOM 653 CA ASN 149 62.475 10.523 20.146 1.00 31.28 ATOM 654 CB ASN 149 62.232 11.613 21.192 1.00 43.55 ATOM 655 CG ASN 149 60.975 12.457 20.898 1.00 55.36 ATOM 656 OD1 ASN 149 60.817 13.032 19.802 1.00 60.56 ATOM 657 ND2 ASN 149 60.085 12.545 21.883 1.00 62.05 ATOM 658 C ASN 149 63.863 9.936 20.299 1.00 27.77 ATOM 659 O ASN 149 64.797 10.369 19.614 1.00 25.49 ATOM 660 N SER 150 63.965 8.917 21.145 1.00 27.48 ATOM 661 CA SER 150 65.212 8.206 21.414 1.00 29.75 ATOM 662 CB SER 150 64.979 7.102 22.445 1.00 32.71 ATOM 663 OG SER 150 64.942 7.628 23.756 1.00 35.48 ATOM 664 C SER 150 65.686 7.543 20.150 1.00 29.64 ATOM 665 O SER 150 66.781 7.814 19.661 1.00 32.57 ATOM 666 N TRP 151 64.841 6.652 19.645 1.00 27.07 ATOM 667 CA TRP 151 65.092 5.909 18.428 1.00 25.09 ATOM 668 CB TRP 151 63.811 5.254 17.953 1.00 24.27 ATOM 669 CG TRP 151 64.046 4.513 16.726 1.00 25.31 ATOM 670 CD2 TRP 151 64.627 3.213 16.629 1.00 26.75 ATOM 671 CE2 TRP 151 64.741 2.911 15.259 1.00 26.58 ATOM 672 CE3 TRP 151 65.068 2.273 17.572 1.00 30.19 ATOM 673 CD1 TRP 151 63.828 4.940 15.455 1.00 23.89 ATOM 674 NE1 TRP 151 64.251 3.984 14.560 1.00 27.19 ATOM 675 CZ2 TRP 151 65.277 1.708 14.804 1.00 31.26 ATOM 676 CZ3 TRP 151 65.600 1.080 17.127 1.00 29.51 ATOM 677 CH2 TRP 151 65.702 0.807 15.754 1.00 32.46 ATOM 678 C TRP 151 65.606 6.787 17.310 1.00 26.40 ATOM 679 O TRP 151 66.545 6.421 16.590 1.00 30.03 ATOM 680 N LYS 152 64.935 7.913 17.111 1.00 27.05 ATOM 681 CA LYS 152 65.321 8.844 16.072 1.00 27.57 ATOM 682 CB LYS 152 64.293 9.955 15.937 1.00 27.96 ATOM 683 CG LYS 152 63.159 9.635 15.008 1.00 30.45 ATOM 684 CD LYS 152 62.571 10.919 14.428 1.00 36.14 ATOM 685 CE LYS 152 61.524 11.548 15.340 1.00 36.97 ATOM 686 NZ LYS 152 61.646 13.036 15.381 1.00 44.84 ATOM 687 C LYS 152 66.694 9.439 16.310 1.00 28.93 ATOM 688 O LYS 152 67.394 9.733 15.345 1.00 26.55 ATOM 689 N LYS 153 67.041 9.670 17.580 1.00 30.64 ATOM 690 CA LYS 153 68.340 10.245 17.974 1.00 36.17 ATOM 691 CB LYS 153 68.280 10.789 19.406 1.00 44.14 ATOM 692 CG LYS 153 67.324 11.951 19.642 1.00 56.90 ATOM 693 CD LYS 153 67.670 12.702 20.941 1.00 62.05 ATOM 694 CE LYS 153 69.028 13.431 20.818 1.00 65.84 ATOM 695 NZ LYS 153 69.403 14.260 22.014 1.00 64.03 ATOM 696 C LYS 153 69.533 9.282 17.935 1.00 34.62 ATOM 697 O LYS 153 70.681 9.709 17.901 1.00 35.40 ATOM 698 N THR 154 69.254 7.989 17.993 1.00 35.88 ATOM 699 CA THR 154 70.279 6.950 18.024 1.00 34.95 ATOM 700 CB THR 154 69.638 5.639 18.516 1.00 35.22 ATOM 701 OG1 THR 154 68.842 5.912 19.685 1.00 39.37 ATOM 702 CG2 THR 154 70.694 4.616 18.877 1.00 38.14 ATOM 703 C THR 154 71.081 6.675 16.748 1.00 34.92 ATOM 704 O THR 154 70.503 6.360 15.704 1.00 34.58 ATOM 705 N PRO 155 72.431 6.800 16.813 1.00 35.68 ATOM 706 CD PRO 155 73.289 7.214 17.941 1.00 32.28 ATOM 707 CA PRO 155 73.245 6.534 15.621 1.00 34.83 ATOM 708 CB PRO 155 74.675 6.588 16.169 1.00 31.93 ATOM 709 CG PRO 155 74.582 7.589 17.249 1.00 30.75 ATOM 710 C PRO 155 72.906 5.122 15.160 1.00 35.09 ATOM 711 O PRO 155 72.585 4.266 15.983 1.00 35.97 ATOM 712 N LEU 156 72.949 4.888 13.852 1.00 40.23 ATOM 713 CA LEU 156 72.653 3.572 13.284 1.00 40.64 ATOM 714 CB LEU 156 72.996 3.536 11.799 1.00 43.18 ATOM 715 CG LEU 156 72.262 4.560 10.936 1.00 46.77 ATOM 716 CD1 LEU 156 72.581 4.315 9.462 1.00 50.39 ATOM 717 CD2 LEU 156 70.763 4.465 11.186 1.00 50.02 ATOM 718 C LEU 156 73.488 2.546 14.004 1.00 40.37 ATOM 719 O LEU 156 72.967 1.569 14.514 1.00 43.12 ATOM 720 N SER 157 74.782 2.832 14.097 1.00 41.57 ATOM 721 CA SER 157 75.768 1.982 14.772 1.00 39.37 ATOM 722 CB SER 157 77.108 2.720 14.810 1.00 42.46 ATOM 723 OG SER 157 76.917 4.128 14.988 1.00 48.99 ATOM 724 C SER 157 75.380 1.580 16.195 1.00 36.81 ATOM 725 O SER 157 75.728 0.495 16.662 1.00 34.45 ATOM 726 N LEU 158 74.646 2.443 16.881 1.00 34.52 ATOM 727 CA LEU 158 74.264 2.133 18.242 1.00 35.24 ATOM 728 CB LEU 158 74.391 3.371 19.121 1.00 33.75 ATOM 729 CG LEU 158 75.760 4.029 19.172 1.00 28.13 ATOM 730 CD1 LEU 158 75.699 5.261 20.058 1.00 28.41 ATOM 731 CD2 LEU 158 76.758 3.025 19.703 1.00 28.88 ATOM 732 C LEU 158 72.877 1.535 18.402 1.00 36.64 ATOM 733 O LEU 158 72.450 1.284 19.530 1.00 43.40 ATOM 734 N ARG 159 72.156 1.315 17.309 1.00 34.12 ATOM 735 CA ARG 159 70.816 0.726 17.416 1.00 34.54 ATOM 736 CB ARG 159 70.002 1.061 16.178 1.00 35.15 ATOM 737 CG ARG 159 69.756 2.533 16.051 1.00 36.06 ATOM 738 CD ARG 159 69.290 2.938 14.676 1.00 35.14 ATOM 739 NE ARG 159 68.887 4.331 14.741 1.00 38.24 ATOM 740 CZ ARG 159 68.047 4.902 13.899 1.00 42.17 ATOM 741 NH1 ARG 159 67.731 6.181 14.043 1.00 44.23 ATOM 742 NH2 ARG 159 67.537 4.191 12.906 1.00 45.95 ATOM 743 C ARG 159 70.886 -0.790 17.653 1.00 32.88 ATOM 744 O ARG 159 71.503 -1.518 16.877 1.00 36.83 ATOM 745 N SER 160 70.249 -1.253 18.723 1.00 27.95 ATOM 746 CA SER 160 70.280 -2.659 19.105 1.00 24.33 ATOM 747 CB SER 160 70.578 -2.744 20.595 1.00 26.10 ATOM 748 OG SER 160 69.572 -2.088 21.356 1.00 24.55 ATOM 749 C SER 160 68.982 -3.386 18.856 1.00 26.96 ATOM 750 O SER 160 67.957 -2.749 18.632 1.00 31.18 ATOM 751 N LYS 161 68.997 -4.713 18.980 1.00 27.03 ATOM 752 CA LYS 161 67.781 -5.503 18.793 1.00 27.02 ATOM 753 CB LYS 161 68.109 -6.990 18.781 1.00 28.66 ATOM 754 CG LYS 161 69.045 -7.392 17.649 1.00 40.43 ATOM 755 CD LYS 161 68.316 -7.505 16.298 1.00 49.88 ATOM 756 CE LYS 161 69.283 -7.711 15.104 1.00 52.99 ATOM 757 NZ LYS 161 68.622 -8.340 13.896 1.00 55.88 ATOM 758 C LYS 161 66.810 -5.196 19.934 1.00 26.74 ATOM 759 O LYS 161 65.596 -5.320 19.789 1.00 25.11 ATOM 760 N ARG 162 67.369 -4.805 21.073 1.00 25.21 ATOM 761 CA ARG 162 66.591 -4.459 22.257 1.00 25.16 ATOM 762 CB ARG 162 67.536 -4.141 23.420 1.00 27.16 ATOM 763 CG ARG 162 66.939 -4.222 24.815 1.00 27.89 ATOM 764 CD ARG 162 67.605 -3.206 25.743 1.00 29.60 ATOM 765 NE ARG 162 67.109 -1.850 25.492 1.00 28.75 ATOM 766 CZ ARG 162 67.830 -0.859 24.963 1.00 30.83 ATOM 767 NH1 ARG 162 69.101 -1.050 24.615 1.00 35.66 ATOM 768 NH2 ARG 162 67.279 0.329 24.765 1.00 21.66 ATOM 769 C ARG 162 65.766 -3.218 21.909 1.00 25.08 ATOM 770 O ARG 162 64.568 -3.169 22.173 1.00 22.87 ATOM 771 N SER 163 66.421 -2.236 21.293 1.00 25.20 ATOM 772 CA SER 163 65.768 -0.997 20.890 1.00 27.25 ATOM 773 CB SER 163 66.762 -0.043 20.233 1.00 28.12 ATOM 774 OG SER 163 67.671 0.494 21.170 1.00 33.02 ATOM 775 C SER 163 64.648 -1.279 19.911 1.00 30.21 ATOM 776 O SER 163 63.576 -0.691 20.009 1.00 35.47 ATOM 777 N GLN 164 64.913 -2.159 18.946 1.00 30.80 ATOM 778 CA GLN 164 63.919 -2.520 17.938 1.00 29.81 ATOM 779 CB GLN 164 64.499 -3.481 16.903 1.00 31.88 ATOM 780 CG GLN 164 65.539 -2.859 15.992 1.00 35.34 ATOM 781 CD GLN 164 65.955 -3.784 14.866 1.00 35.38 ATOM 782 OE1 GLN 164 66.055 -4.994 15.049 1.00 36.50 ATOM 783 NE2 GLN 164 66.185 -3.219 13.690 1.00 37.36 ATOM 784 C GLN 164 62.723 -3.176 18.588 1.00 27.06 ATOM 785 O GLN 164 61.599 -2.696 18.465 1.00 28.49 ATOM 786 N ASP 165 62.984 -4.290 19.260 1.00 27.83 ATOM 787 CA ASP 165 61.962 -5.043 19.956 1.00 28.49 ATOM 788 CB ASP 165 62.588 -6.148 20.822 1.00 33.50 ATOM 789 CG ASP 165 63.140 -7.321 20.004 1.00 38.35 ATOM 790 OD1 ASP 165 62.828 -7.442 18.802 1.00 43.20 ATOM 791 OD2 ASP 165 63.886 -8.152 20.573 1.00 41.86 ATOM 792 C ASP 165 61.123 -4.118 20.820 1.00 28.33 ATOM 793 O ASP 165 59.900 -4.146 20.719 1.00 29.40 ATOM 794 N ARG 166 61.748 -3.267 21.635 1.00 26.02 ATOM 795 CA ARG 166 60.928 -2.404 22.453 1.00 30.80 ATOM 796 CB ARG 166 61.638 -1.826 23.703 1.00 41.63 ATOM 797 CG ARG 166 62.815 -0.854 23.491 1.00 63.41 ATOM 798 CD ARG 166 62.451 0.565 22.887 1.00 74.62 ATOM 799 NE ARG 166 63.602 1.218 22.219 1.00 79.94 ATOM 800 CZ ARG 166 63.505 2.185 21.299 1.00 80.41 ATOM 801 NH1 ARG 166 64.607 2.721 20.751 1.00 81.58 ATOM 802 NH2 ARG 166 62.308 2.607 20.911 1.00 81.81 ATOM 803 C ARG 166 60.132 -1.356 21.699 1.00 29.00 ATOM 804 O ARG 166 58.930 -1.280 21.909 1.00 29.60 ATOM 805 N ILE 167 60.738 -0.608 20.777 1.00 26.06 ATOM 806 CA ILE 167 59.963 0.394 20.066 1.00 23.75 ATOM 807 CB ILE 167 60.810 1.191 19.093 1.00 20.38 ATOM 808 CG2 ILE 167 61.452 0.280 18.112 1.00 25.06 ATOM 809 CG1 ILE 167 59.951 2.228 18.385 1.00 20.43 ATOM 810 CD1 ILE 167 60.140 3.600 18.837 1.00 18.35 ATOM 811 C ILE 167 58.753 -0.248 19.363 1.00 28.10 ATOM 812 O ILE 167 57.628 0.240 19.495 1.00 29.42 ATOM 813 N ARG 168 58.945 -1.384 18.698 1.00 28.88 ATOM 814 CA ARG 168 57.817 -2.048 18.033 1.00 32.17 ATOM 815 CB ARG 168 58.232 -3.386 17.437 1.00 31.63 ATOM 816 CG ARG 168 58.640 -3.323 16.009 1.00 37.29 ATOM 817 CD ARG 168 58.832 -4.719 15.462 1.00 37.37 ATOM 818 NE ARG 168 60.200 -5.185 15.647 1.00 34.57 ATOM 819 CZ ARG 168 60.529 -6.378 16.122 1.00 33.36 ATOM 820 NH1 ARG 168 61.810 -6.699 16.249 1.00 34.45 ATOM 821 NH2 ARG 168 59.584 -7.235 16.487 1.00 35.04 ATOM 822 C ARG 168 56.674 -2.321 19.000 1.00 34.64 ATOM 823 O ARG 168 55.541 -1.914 18.769 1.00 39.25 ATOM 824 N GLU 169 56.998 -3.021 20.079 1.00 37.29 ATOM 825 CA GLU 169 56.059 -3.410 21.129 1.00 39.87 ATOM 826 CB GLU 169 56.860 -3.956 22.320 1.00 48.72 ATOM 827 CG GLU 169 56.049 -4.600 23.449 1.00 55.06 ATOM 828 CD GLU 169 56.945 -5.101 24.578 1.00 57.67 ATOM 829 OE1 GLU 169 57.900 -4.379 24.949 1.00 55.59 ATOM 830 OE2 GLU 169 56.692 -6.214 25.091 1.00 58.16 ATOM 831 C GLU 169 55.181 -2.250 21.580 1.00 36.09 ATOM 832 O GLU 169 54.004 -2.425 21.898 1.00 33.57 ATOM 833 N LEU 170 55.781 -1.069 21.615 1.00 32.71 ATOM 834 CA LEU 170 55.093 0.135 22.005 1.00 29.32 ATOM 835 CB LEU 170 56.097 1.231 22.321 1.00 27.42 ATOM 836 CG LEU 170 56.464 1.321 23.795 1.00 29.26 ATOM 837 CD1 LEU 170 57.580 2.378 24.032 1.00 20.06 ATOM 838 CD2 LEU 170 55.165 1.641 24.552 1.00 25.26 ATOM 839 C LEU 170 54.197 0.595 20.893 1.00 28.58 ATOM 840 O LEU 170 53.050 0.943 21.135 1.00 37.18 ATOM 841 N PHE 171 54.709 0.611 19.671 1.00 24.66 ATOM 842 CA PHE 171 53.899 1.063 18.563 1.00 22.29 ATOM 843 CB PHE 171 54.699 1.053 17.247 1.00 19.78 ATOM 844 CG PHE 171 53.874 1.411 16.018 1.00 17.53 ATOM 845 CD1 PHE 171 53.766 2.731 15.590 1.00 11.80 ATOM 846 CD2 PHE 171 53.148 0.422 15.330 1.00 14.77 ATOM 847 CE1 PHE 171 52.941 3.067 14.504 1.00 11.46 ATOM 848 CE2 PHE 171 52.315 0.758 14.242 1.00 10.44 ATOM 849 CZ PHE 171 52.214 2.085 13.836 1.00 6.72 ATOM 850 C PHE 171 52.659 0.183 18.471 1.00 21.88 ATOM 851 O PHE 171 51.556 0.693 18.381 1.00 23.54 ATOM 852 N SER 172 52.839 -1.129 18.540 1.00 23.14 ATOM 853 CA SER 172 51.729 -2.069 18.428 1.00 27.99 ATOM 854 CB SER 172 52.228 -3.504 18.485 1.00 27.59 ATOM 855 OG SER 172 53.331 -3.669 17.624 1.00 31.04 ATOM 856 C SER 172 50.751 -1.875 19.547 1.00 33.07 ATOM 857 O SER 172 49.564 -2.166 19.392 1.00 38.22 ATOM 858 N GLN 173 51.276 -1.425 20.684 1.00 36.24 ATOM 859 CA GLN 173 50.509 -1.166 21.903 1.00 37.57 ATOM 860 CB GLN 173 51.499 -0.888 23.068 1.00 44.34 ATOM 861 CG GLN 173 50.894 -0.718 24.476 1.00 54.23 ATOM 862 CD GLN 173 51.291 -1.831 25.447 1.00 60.34 ATOM 863 OE1 GLN 173 51.402 -1.609 26.659 1.00 57.52 ATOM 864 NE2 GLN 173 51.482 -3.040 24.921 1.00 66.46 ATOM 865 C GLN 173 49.557 0.031 21.692 1.00 32.96 ATOM 866 O GLN 173 48.324 -0.078 21.833 1.00 30.70 ATOM 867 N ALA 174 50.142 1.166 21.342 1.00 25.13 ATOM 868 CA ALA 174 49.371 2.356 21.124 1.00 23.49 ATOM 869 CB ALA 174 50.288 3.499 20.814 1.00 20.35 ATOM 870 C ALA 174 48.368 2.139 20.008 1.00 22.23 ATOM 871 O ALA 174 47.176 2.342 20.208 1.00 28.71 ATOM 872 N GLU 175 48.833 1.646 18.866 1.00 23.39 ATOM 873 CA GLU 175 47.973 1.415 17.700 1.00 24.62 ATOM 874 CB GLU 175 48.790 0.901 16.506 1.00 23.76 ATOM 875 CG GLU 175 48.055 0.935 15.154 1.00 28.00 ATOM 876 CD GLU 175 47.069 -0.208 14.953 1.00 24.81 ATOM 877 OE1 GLU 175 47.415 -1.356 15.249 1.00 30.25 ATOM 878 OE2 GLU 175 45.944 0.031 14.499 1.00 25.54 ATOM 879 C GLU 175 46.815 0.465 17.975 1.00 23.05 ATOM 880 O GLU 175 45.680 0.718 17.549 1.00 23.75 ATOM 881 N SER 176 47.117 -0.658 18.610 1.00 23.70 ATOM 882 CA SER 176 46.093 -1.633 18.939 1.00 25.29 ATOM 883 CB SER 176 46.720 -2.904 19.483 1.00 27.82 ATOM 884 OG SER 176 45.715 -3.746 20.007 1.00 37.64 ATOM 885 C SER 176 45.113 -1.066 19.955 1.00 27.15 ATOM 886 O SER 176 43.911 -1.266 19.827 1.00 29.62 ATOM 887 N HIS 177 45.616 -0.343 20.953 1.00 27.84 ATOM 888 CA HIS 177 44.736 0.231 21.947 1.00 29.40 ATOM 889 CB HIS 177 45.525 0.880 23.083 1.00 35.05 ATOM 890 CG HIS 177 44.670 1.358 24.221 1.00 39.71 ATOM 891 CD2HIS 177 43.330 1.519 24.331 1.00 39.99 ATOM 892 ND1 HIS 177 45.195 1.730 25.442 1.00 45.29 ATOM 893CE1 HIS 177 44.215 2.098 26.251 1.00 43.30 ATOM 894 NE2 HIS 177 43.072 1.979 25.598 1.00 41.68 ATOM 895 C HIS 177 43.827 1.248 21.262 1.00 31.02 ATOM 896 O HIS 177 42.624 1.300 21.534 1.00 35.22 ATOM 897 N PHE 178 44.369 2.050 20.359 1.00 28.97 ATOM 898 CA PHE 178 43.525 3.023 19.683 1.00 28.86 ATOM 899 CB PHE 178 44.358 3.929 18.779 1.00 25.66 ATOM 900 CG PHE 178 44.816 5.209 19.441 1.00 22.69 ATOM 901 CD1 PHE 178 46.085 5.312 19.993 1.00 25.93 ATOM 902 CD2 PHE 178 44.019 6.347 19.411 1.00 23.46 ATOM 903 CE1 PHE 178 46.560 6.537 20.490 1.00 20.31 ATOM 904 CE2 PHE 178 44.485 7.567 19.906 1.00 21.41 ATOM 905 CZ PHE 178 45.757 7.654 20.439 1.00 21.04 ATOM 906 C PHE 178 42.457 2.290 18.875 1.00 29.52 ATOM 907 O PHE 178 41.268 2.545 19.022 1.00 25.37 ATOM 908 N ARG 179 42.888 1.299 18.105 1.00 32.49 ATOM 909 CA ARG 179 41.989 0.525 17.269 1.00 30.66 ATOM 910 CB ARG 179 42.733 -0.654 16.646 1.00 31.64 ATOM 911 CG ARG 179 41.976 -1.291 15.519 1.00 34.21 ATOM 912 CD ARG 179 42.831 -2.263 14.759 1.00 41.71 ATOM 913 NE ARG 179 42.897 -3.560 15.417 1.00 45.91 ATOM 914 CZ ARG 179 44.010 -4.095 15.909 1.00 52.23 ATOM 915 NH1 ARG 179 45.166 -3.448 15.815 1.00 48.56 ATOM 916 NH2 ARG 179 43.961 -5.278 16.518 1.00 60.56 ATOM 917 C ARG 179 40.780 0.018 18.026 1.00 29.30 ATOM 918 O ARG 179 39.656 0.169 17.574 1.00 34.87 ATOM 919 N ASN 180 41.004 -0.537 19.201 1.00 29.94 ATOM 920 CA ASN 180 39.911 -1.077 19.992 1.00 32.10 ATOM 921 CB ASN 180 40.418 -2.277 20.804 1.00 36.87 ATOM 922 CG ASN 180 41.000 -3.393 19.917 1.00 38.96 ATOM 923 OD1 ASN 180 40.358 -3.861 18.981 1.00 40.44 ATOM 924 ND2 ASN 180 42.214 -3.821 20.224 1.00 42.74 ATOM 925 C ASN 180 39.125 -0.073 20.875 1.00 32.03 ATOM 926 O ASN 180 38.036 -0.387 21.337 1.00 34.18 ATOM 927 N SER 181 39.661 1.126 21.106 1.00 32.59 ATOM 928 CA SER 181 38.965 2.150 21.904 1.00 26.92 ATOM 929 CB SER 181 39.939 3.211 22.429 1.00 27.48 ATOM 930 OG SER 181 40.884 2.658 23.324 1.00 31.01 ATOM 931 C SER 181 37.883 2.902 21.134 1.00 25.45 ATOM 932 O SER 181 36.871 3.288 21.705 1.00 25.81 ATOM 933 N MET 182 38.111 3.143 19.847 1.00 23.99 ATOM 934 CA MET 182 37.169 3.898 19.014 1.00 24.66 ATOM 935 CB MET 182 37.418 3.676 17.519 1.00 25.35 ATOM 936 CG MET 182 38.588 4.436 16.936 1.00 22.11 ATOM 937 SD MET 182 38.582 6.169 17.397 1.00 31.27 ATOM 938 CE MET 182 40.288 6.254 17.748 1.00 28.60 ATOM 939 C MET 182 35.697 3.699 19.298 1.00 22.86 ATOM 940 O MET 182 34.946 4.674 19.354 1.00 26.55 ATOM 941 N PRO 183 35.257 2.448 19.504 1.00 20.02 ATOM 942 CD PRO 183 35.911 1.131 19.367 1.00 17.72 ATOM 943 CA PRO 183 33.814 2.311 19.771 1.00 20.18 ATOM 944 CB PRO 183 33.626 0.790 19.918 1.00 19.03 ATOM 945 CG PRO 183 34.758 0.210 19.057 1.00 15.96 ATOM 946 C PRO 183 33.306 3.109 20.990 1.00 21.68 ATOM 947 O PRO 183 32.167 3.557 20.995 1.00 27.17 ATOM 948 N SER 184 34.166 3.342 21.986 1.00 22.98 ATOM 949 CA SER 184 33.813 4.107 23.186 1.00 18.39 ATOM 950 CB SER 184 34.968 4.066 24.198 1.00 15.92 ATOM 951 OG SER 184 35.328 2.729 24.522 1.00 15.22 ATOM 952 C SER 184 33.432 5.568 22.895 1.00 21.41 ATOM 953 O SER 184 32.924 6.254 23.776 1.00 17.59 ATOM 954 N PHE 185 33.702 6.057 21.682 1.00 20.87 ATOM 955 CA PHE 185 33.367 7.435 21.342 1.00 21.72 ATOM 956 CB PHE 185 34.591 8.195 20.843 1.00 19.91 ATOM 957 CG PHE 185 35.865 7.857 21.578 1.00 23.10 ATOM 958 CD1 PHE 185 37.033 7.561 20.875 1.00 20.78 ATOM 959 CD2 PHE 185 35.909 7.840 22.960 1.00 19.79 ATOM 960 CE1 PHE 185 38.226 7.252 21.546 1.00 23.07 ATOM 961 CE2 PHE 185 37.106 7.529 23.633 1.00 25.58 ATOM 962 CZ PHE 185 38.262 7.235 22.920 1.00 16.31 ATOM 963 C PHE 185 32.306 7.429 20.261 1.00 24.33 ATOM 964 O PHE 185 32.075 8.432 19.599 1.00 24.66 ATOM 965 N ALA 186 31.613 6.306 20.134 1.00 28.12 ATOM 966 CA ALA 186 30.581 6.146 19.116 1.00 27.05 ATOM 967 CB ALA 186 31.189 5.473 17.870 1.00 29.72 ATOM 968 C ALA 186 29.469 5.283 19.684 1.00 26.76 ATOM 969 O ALA 186 28.840 4.492 18.969 1.00 26.03 ATOM 970 N VAL 187 29.265 5.415 20.986 1.00 27.16 ATOM 971 CA VAL 187 28.238 4.661 21.689 1.00 29.69 ATOM 972 CB VAL 187 28.175 5.047 23.170 1.00 29.53 ATOM 973 CG1 VAL 187 27.451 3.986 23.923 1.00 32.69 ATOM 974 CG2 VAL 187 29.555 5.282 23.730 1.00 31.55 ATOM 975 C VAL 187 26.867 4.963 21.092 1.00 30.99 ATOM 976 O VAL 187 26.544 6.121 20.818 1.00 32.51 ATOM 977 N SER 188 26.045 3.933 20.944 1.00 33.95 ATOM 978 CA SER 188 24.703 4.094 20.392 1.00 39.13 ATOM 979 CB SER 188 23.924 2.782 20.524 1.00 37.12 ATOM 980 OG SER 188 23.056 2.573 19.415 1.00 42.00 ATOM 981 C SER 188 23.960 5.228 21.104 1.00 40.12 ATOM 982 O SER 188 24.106 5.401 22.316 1.00 42.73 ATOM 983 N LYS 189 23.231 6.038 20.338 1.00 42.68 ATOM 984 CA LYS 189 22.468 7.158 20.883 1.00 43.93 ATOM 985 CB LYS 189 21.718 6.715 22.151 1.00 51.42 ATOM 986 CG LYS 189 20.770 7.737 22.743 1.00 65.46 ATOM 987 CD LYS 189 20.195 7.249 24.074 1.00 75.80 ATOM 988 CE LYS 189 19.366 8.343 24.769 1.00 83.02 ATOM 989 NZ LYS 189 18.929 7.964 26.159 1.00 86.33 ATOM 990 C LYS 189 23.322 8.395 21.177 1.00 39.73 ATOM 991 O LYS 189 22.799 9.507 21.251 1.00 40.92 ATOM 992 N PHE 190 24.633 8.220 21.297 1.00 36.45 ATOM 993 CA PHE 190 25.532 9.339 21.596 1.00 32.97 ATOM 994 CB PHE 190 26.266 9.053 22.906 1.00 35.66 ATOM 995 CG PHE 190 25.349 8.799 24.059 1.00 37.16 ATOM 996 CD1 PHE 190 25.169 7.510 24.544 1.00 37.15 ATOM 997 CD2 PHE 190 24.620 9.841 24.623 1.00 37.31 ATOM 998 CE1 PHE 190 24.279 7.259 25.568 1.00 36.95 ATOM 999 CE2 PHE 190 23.722 9.602 25.652 1.00 37.94 ATOM 1000 CZ PHE 190 23.551 8.310 26.124 1.00 37.75 ATOM 1001 C PHE 190 26.554 9.640 20.499 1.00 28.22 ATOM 1002 O PHE 190 27.573 10.285 20.746 1.00 27.75 ATOM 1003 N GLU 191 26.270 9.210 19.280 1.00 27.87 ATOM 1004 CA GLU 191 27.212 9.420 18.196 1.00 25.18 ATOM 1005 CB GLU 191 26.823 8.642 16.961 1.00 23.69 ATOM 1006 CG GLU 191 26.809 7.147 17.187 1.00 25.09 ATOM 1007 CD GLU 191 25.416 6.613 17.376 1.00 26.96 ATOM 1008 OE1 GLU 191 25.157 5.496 16.884 1.00 31.29 ATOM 1009 OE2 GLU 191 24.575 7.304 18.090 1.00 27.39 ATOM 1010 C GLU 191 27.439 10.865 17.869 1.00 25.02 ATOM 1011 O GLU 191 28.576 11.247 17.631 1.00 27.85 ATOM 1012N VAL 192 26.391 11.686 17.898 1.00 27.84 ATOM 1013 CA VAL 192 26.557 13.114 17.620 1.00 25.95 ATOM 1014 CB VAL 192 25.232 13.804 17.352 1.00 26.44 ATOM 1015 CG1 VAL 192 25.468 15.283 17.037 1.00 24.26 ATOM 1016 CG2 VAL 192 24.489 13.089 16.240 1.00 22.90 ATOM 1017 C VAL 192 27.245 13.824 18.793 1.00 28.20 ATOM 1018 O VAL 192 28.198 14.584 18.605 1.00 33.10 ATOM 1019 N LEU 193 26.805 13.541 20.010 1.00 24.52 ATOM 1020 CA LEU 193 27.408 14.174 21.178 1.00 25.78 ATOM 1021 CB LEU 193 26.669 13.706 22.436 1.00 25.22 ATOM 1022CG LEU 193 25.241 14.207 22.612 1.00 17.24 ATOM 1023 CD1 LEU 193 24.489 13.345 23.599 1.00 24.15 ATOM 1024 CD2 LEU 193 25.303 15.634 23.111 1.00 22.79 ATOM 1025 C LEU 193 28.936 13.937 21.316 1.00 27.53 ATOM 1026 O LEU 193 29.675 14.798 21.835 1.00 22.52 ATOM 1027 N PHE 194 29.394 12.767 20.860 1.00 28.95 ATOM 1028 CA PHE 194 30.809 12.371 20.912 1.00 27.24 ATOM 1029 CB PHE 194 30.926 10.838 21.023 1.00 23.99 ATOM 1030 CG PHE 194 30.883 10.302 22.424 1.00 19.23 ATOM 1031 CD1 PHE 194 29.946 9.331 22.771 1.00 16.74 ATOM 1032 CD2 PHE 194 31.806 10.734 23.381 1.00 12.01 ATOM 1033 CE1 PHE 194 29.924 8.790 24.058 1.00 20.23 ATOM 1034 CE2 PHE 194 31.807 10.213 24.670 1.00 15.47 ATOM 1035 CZ PHE 194 30.862 9.233 25.019 1.00 21.85 ATOM 1036 C PHE 194 31.597 12.769 19.653 1.00 30.35 ATOM 1037 O PHE 194 32.771 12.413 19.540 1.00 33.71 ATOM 1038 N LEU 195 30.990 13.512 18.730 1.00 27.41 ATOM 1039 CA LEU 195 31.659 13.845 17.466 1.00 23.44 ATOM 1040 CB LEU 195 30.755 14.704 16.592 1.00 24.37 ATOM 1041 CG LEU 195 30.899 14.393 15.109 1.00 30.12 ATOM 1042 CD1 LEU 195 30.651 12.891 14.842 1.00 26.11 ATOM 1043 CD2 LEU 195 29.922 15.244 14.338 1.00 30.52 ATOM 1044 C LEU 195 33.074 14.407 17.465 1.00 18.68 ATOM 1045 O LEU 195 33.954 13.869 16.809 1.00 20.43 ATOM 1046 N PRO 196 33.316 15.503 18.173 1.00 16.00 ATOM 1047 CD PRO 196 32.351 16.380 18.850 1.00 13.80 ATOM 1048 CA PRO 196 34.668 16.072 18.193 1.00 14.01 ATOM 1049 CB PRO 196 34.491 17.343 18.993 1.00 14.53 ATOM 1050 CG PRO 196 33.026 17.698 18.756 1.00 16.77 ATOM 1051 C PRO 196 35.683 15.150 18.848 1.00 17.13 ATOM 1052 O PRO 196 36.828 15.048 18.395 1.00 19.94 ATOM 1053 N THR 197 35.268 14.499 19.929 1.00 18.61 ATOM 1054 CA THR 197 36.118 13.557 20.659 1.00 20.79 ATOM 1055 CB THR 197 35.320 12.890 21.797 1.00 24.29 ATOM 1056 OG1 THR 197 34.828 13.892 22.688 1.00 26.50 ATOM 1057 CG2 THR 197 36.182 11.905 22.554 1.00 20.17 ATOM 1058 C THR 197 36.588 12.453 19.699 1.00 23.61 ATOM 1059 O THR 197 37.780 12.111 19.663 1.00 26.22 ATOM 1060 N TYR 198 35.631 11.891 18.946 1.00 21.68 ATOM 1061 CA TYR 198 35.870 10.837 17.953 1.00 15.60 ATOM 1062 CB TYR 198 34.545 10.373 17.342 1.00 12.95 ATOM 1063 CG TYR 198 34.661 9.276 16.294 1.00 18.00 ATOM 1064 CD1 TYR 198 34.391 7.946 16.613 1.00 14.34 ATOM 1065 CE1 TYR 198 34.482 6.948 15.659 1.00 21.67 ATOM 1066 CD2 TYR 198 35.029 9.569 14.975 1.00 20.14 ATOM 1067 CE2 TYR 198 35.121 8.564 14.010 1.00 20.73 ATOM 1068 CZ TYR 198 34.848 7.268 14.360 1.00 18.41 ATOM 1069 OH TYR 198 34.917 6.287 13.407 1.00 24.92 ATOM 1070 C TYR 198 36.807 11.342 16.850 1.00 19.32 ATOM 1071 O TYR 198 37.813 10.700 16.554 1.00 19.54 ATOM 1072 N ALA 199 36.494 12.487 16.251 1.00 14.36 ATOM 1073 CA ALA 199 37.342 13.020 15.205 1.00 14.32 ATOM 1074 CB ALA 199 36.818 14.357 14.748 1.00 16.43 ATOM 1075 C ALA 199 38.789 13.146 15.694 1.00 16.89 ATOM 1076 O ALA 199 39.714 12.639 15.044 1.00 16.56 ATOM 1077 N GLN 200 38.964 13.765 16.868 1.00 18.58 ATOM 1078 CA GLN 200 40.281 13.984 17.492 1.00 18.04 ATOM 1079 CB GLN 200 40.151 14.844 18.744 1.00 16.98 ATOM 1080 CG GLN 200 39.629 16.239 18.489 1.00 16.64 ATOM 1081 CD GLN 200 40.593 17.109 17.709 1.00 17.76 ATOM 1082 CE1 GLN 200 41.811 16.965 17.821 1.00 20.73 ATOM 1083 NE2 GLN 200 40.051 18.032 16.926 1.00 16.40 ATOM 1084 C GLN 200 41.067 12.721 17.833 1.00 16.13 ATOM 1085 O GLN 200 42.287 12.732 17.758 1.00 18.50 ATOM 1086 N ALA 201 40.393 11.665 18.276 1.00 15.14 ATOM 1087 CA ALA 201 41.093 10.414 18.578 1.00 15.80 ATOM 1088 CB ALA 201 40.244 9.507 19.463 1.00 11.71 ATOM 1089 C ALA 201 41.447 9.696 17.277 1.00 15.73 ATOM 1090 O ALA 201 42.521 9.110 17.155 1.00 23.19 ATOM 1091 N ALA 202 40.528 9.724 16.315 1.00 16.63 ATOM 1092 CA ALA 202 40.714 9.105 15.007 1.00 10.64 ATOM 1093 CB ALA 202 39.519 9.386 14.120 1.00 12.27 ATOM 1094 C ALA 202 41.954 9.686 14.376 1.00 11.25 ATOM 1095 O ALA 202 42.855 8.966 13.963 1.00 12.02 ATOM 1096 N ASN 203 42.005 11.005 14.328 1.00 10.25 ATOM 1097 CA ASN 203 43.143 11.684 13.767 1.00 14.32 ATOM 1098 CB ASN 203 43.015 13.167 14.008 1.00 14.52 ATOM 1099 CG ASN 203 44.207 13.926 13.501 1.00 15.52 ATOM 1100 OD1 ASN 203 44.459 13.939 12.310 1.00 23.18 ATOM 1101 ND2 ASN 203 44.934 14.566 14.390 1.00 12.62 ATOM 1102 C ASN 203 44.473 11.205 14.338 1.00 19.00 ATOM 1103 O ASN 203 45.457 11.116 13.613 1.00 27.47 ATOM 1104 N THR 204 44.518 10.882 15.628 1.00 19.90 ATOM 1105 CA THR 204 45.765 10.433 16.249 1.00 19.76 ATOM 1106 CB THR 204 45.691 10.527 17.761 1.00 19.43 ATOM 1107 OG1 THR 204 45.409 11.882 18.129 1.00 23.03 ATOM 1108 CG2 THR 204 47.001 10.115 18.364 1.00 22.47 ATOM 1109 C THR 204 46.119 9.008 15.851 1.00 20.39 ATOM 1110 O THR 204 47.300 8.673 15.663 1.00 11.64 ATOM 1111 N HIS 205 45.079 8.179 15.718 1.00 15.29 ATOM 1112 CA HIS 205 45.246 6.793 15.329 1.00 12.93 ATOM 1113 CB HIS 205 43.890 6.119 15.300 1.00 9.41 ATOM 1114 CG HIS 205 43.960 4.648 15.077 1.00 11.32 ATOM 1115 CD2 HIS 205 45.012 3.796 15.056 1.00 12.67 ATOM 1116 ND1 HIS 205 42.842 3.881 14.841 1.00 11.26 ATOM 1117 CE1 HIS 205 43.198 2.616 14.686 1.00 11.39 ATOM 1118 NE2 HIS 205 44.509 2.536 14.810 1.00 10.23 ATOM 1119 C HIS 205 45.914 6.731 13.954 1.00 14.03 ATOM 1120 O HIS 205 46.788 5.912 13.711 1.00 17.30 ATOM 1121 N LEU 206 45.471 7.605 13.063 1.00 17.93 ATOM 1122 CA LEU 206 45.988 7.716 11.705 1.00 20.38 ATOM 1123 CB LEU 206 45.030 8.552 10.837 1.00 15.00 ATOM 1124 CG LEU 206 43.611 7.985 10.669 1.00 17.79 ATOM 1125 CD1 LEU 206 42.902 8.815 9.643 1.00 16.39 ATOM 1126 CD2 LEU 206 43.606 6.519 10.256 1.00 7.72 ATOM 1127 C LEU 206 47.394 8.333 11.670 1.00 22.16 ATOM 1128 O LEU 206 48.260 7.964 10.811 1.00 26.75 ATOM 1129 N LEU 207 47.652 9.315 12.541 1.00 18.99 ATOM 1130 CA LEU 207 48.959 9.965 12.637 1.00 17.75 ATOM 1131 CB LEU 207 48.953 11.016 13.716 1.00 18.85 ATOM 1132 CG LEU 207 48.829 12.451 13.261 1.00 26.70 ATOM 1133 CD1 LEU 207 48.941 13.280 14.541 1.00 20.06 ATOM 1134 CD2 LEU 207 49.924 12.829 12.198 1.00 20.90 ATOM 1135 C LEU 207 49.982 8.960 13.077 1.00 19.69 ATOM 1136 O LEU 207 51.156 9.075 12.767 1.00 25.73 ATOM 1137 N LEU 208 49.534 8.035 13.901 1.00 20.55 ATOM 1138 CA LEU 208 50.377 6.989 14.433 1.00 21.59 ATOM 1139 CB LEU 208 49.719 6.449 15.683 1.00 22.51 ATOM 1140 CG LEU 208 50.338 5.240 16.322 1.00 25.67 ATOM 1141 CD1 LEU 208 51.707 5.621 16.833 1.00 25.95 ATOM 1142 CD2 LEU 208 49.403 4.792 17.428 1.00 24.34 ATOM 1143 C LEU 208 50.607 5.874 13.411 1.00 21.91 ATOM 1144 O LEU 208 51.758 5.505 13.173 1.00 25.74 ATOM 1145 N LEU 209 49.535 5.367 12.787 1.00 19.26 ATOM 1146 CA LEU 209 49.635 4.286 11.777 1.00 16.77 ATOM 1147 CB LEU 209 48.271 3.966 11.168 1.00 13.38 ATOM 1148 CG LEU 209 47.330 3.000 11.874 1.00 13.06 ATOM 1149 CD1 LEU 209 45.921 3.206 11.379 1.00 7.67 ATOM 1150 CD2 LEU 209 47.779 1.568 11.664 1.00 14.89 ATOM 1151 C LEU 209 50.621 4.596 10.639 1.00 16.38 ATOM 1152 O LEU 209 51.370 3.721 10.186 1.00 17.07 ATOM 1153 N LYS 210 50.635 5.842 10.187 1.00 13.88 ATOM 1154 CA LYS 210 51.536 6.208 9.129 1.00 14.30 ATOM 1155 CB LYS 210 51.220 7.624 8.608 1.00 11.99 ATOM 1156 CG LYS 210 51.477 8.779 9.526 1.00 7.35 ATOM 1157 CD LYS 210 52.797 9.443 9.221 1.00 6.42 ATOM 1158 CE LYS 210 53.002 10.669 10.085 1.00 6.47 ATOM 1159 NZ LYS 210 53.263 10.313 11.513 1.00 14.19 ATOM 1160 C LYS 210 53.008 6.020 9.523 1.00 17.24 ATOM 1161 O LYS 210 53.845 5.688 8.670 1.00 21.95 ATOM 1162 N ASP 211 53.306 6.139 10.819 1.00 19.90 ATOM 1163 CA ASP 211 54.670 5.983 11.336 1.00 16.45 ATOM 1164 CB ASP 211 54.685 6.109 12.854 1.00 11.34 ATOM 1165 CG ASP 211 54.823 7.529 13.326 1.00 13.51 ATOM 1166 OD1 ASP 211 55.048 8.445 12.522 1.00 11.47 ATOM 1167 OD2 ASP 211 54.742 7.740 14.545 1.00 19.85 ATOM 1168 C ASP 211 55.219 4.628 10.945 1.00 16.72 ATOM 1169 O ASP 211 56.424 4.461 10.749 1.00 21.07 ATOM 1170 N ALA 212 54.307 3.679 10.778 1.00 15.96 ATOM 1171 CA ALA 212 54.638 2.317 10.395 1.00 13.35 ATOM 1172 CB ALA 212 53.406 1.453 10.450 1.00 9.60 ATOM 1173 C ALA 212 55.246 2.251 9.001 1.00 17.10 ATOM 1174 O ALA 212 56.055 1.368 8.735 1.00 21.49 ATOM 1175 N GLN 213 54.860 3.181 8.122 1.00 17.33 ATOM 1176 CA GLN 213 55.345 3.228 6.740 1.00 14.16 ATOM 1177 CB GLN 213 54.295 3.896 5.838 1.00 13.57 ATOM 1178 CG GLN 213 52.895 3.233 5.913 1.00 8.05 ATOM 1179 CD GLN 213 52.956 1.733 5.680 1.00 9.09 ATOM 1180 OE1 GLN 213 53.641 1.288 4.777 1.00 13.24 ATOM 1181 NE2 GLN 213 52.284 0.950 6.518 1.00 7.98 ATOM 1182 C GLN 213 56.681 3.948 6.661 1.00 17.76 ATOM 1183 O GLN 213 57.479 3.716 5.752 1.00 22.36 ATOM 1184 N VAL 214 56.918 4.838 7.614 1.00 16.49 ATOM 1185 CA VAL 214 58.181 5.567 7.689 1.00 16.94 ATOM 1186 CB VAL 214 58.008 6.922 8.418 1.00 17.23 ATOM 1187 CG1 VAL 214 59.328 7.615 8.598 1.00 17.53 ATOM 1188 CG2 VAL 214 57.076 7.809 7.631 1.00 17.23 ATOM 1189 C VAL 214 59.261 4.731 8.396 1.00 15.03 ATOM 1190 O VAL 214 60.314 4.506 7.833 1.00 12.50 ATOM 1191 N PHE 215 58.961 4.188 9.576 1.00 18.28 ATOM 1192 CA PHE 215 59.943 3.422 10.350 1.00 13.37 ATOM 1193 CB PHE 215 59.892 3.849 11.805 1.00 14.35 ATOM 1194 CG PHE 215 60.044 5.306 12.011 1.00 12.08 ATOM 1195 CD1 PHE 215 58.932 6.092 12.281 1.00 13.84 ATOM 1196 CD2 PHE 215 61.284 5.903 11.895 1.00 11.02 ATOM 1197 CE1 PHE 215 59.052 7.459 12.425 1.00 11.98 ATOM 1198 CE2 PHE 215 61.420 7.264 12.038 1.00 16.66 ATOM 1199 CZ PHE 215 60.294 8.052 12.302 1.00 17.15 ATOM 1200 C PHE 215 59.854 1.906 10.341 1.00 15.97 ATOM 1201 O PHE 215 60.826 1.243 10.675 1.00 19.35 ATOM 1202 N GLY 216 58.700 1.355 9.981 1.00 16.28 ATOM 1203 CA GLY 216 58.505 -0.087 9.975 1.00 16.57 ATOM 1204 C GLY 216 59.707 -0.955 9.654 1.00 21.88 ATOM 1205 O GLY 216 60.073 -1.849 10.433 1.00 19.41 ATOM 1206 N GLU 217 60.342 -0.672 8.521 1.00 24.90 ATOM 1207 CA GLU 217 61.488 -1.439 8.085 1.00 28.00 ATOM 1208 CB GLU 217 61.919 -1.027 6.688 1.00 35.93 ATOM 1209 CG GLU 217 63.039 -1.914 6.163 1.00 51.31 ATOM 1210 CD GLU 217 63.279 -1.749 4.683 1.00 59.93 ATOM 1211 OE1 GLU 217 62.298 -1.817 3.904 1.00 65.77 ATOM 1212 OE2 GLU 217 64.456 -1.556 4.302 1.00 68.04 ATOM 1213 C GLU 217 62.679 -1.407 9.025 1.00 27.28 ATOM 1214 O GLU 217 63.299 -2.446 9.260 1.00 31.56 ATOM 1215 N GLU 218 63.029 -0.229 9.535 1.00 22.80 ATOM 1216 CA GLU 218 64.149 -0.126 10.462 1.00 19.69 ATOM 1217 CB GLU 218 64.705 1.302 10.527 1.00 19.03 ATOM 1218 CG GLU 218 63.743 2.371 10.982 1.00 23.93 ATOM 1219 CD GLU 218 64.270 3.783 10.738 1.00 31.49 ATOM 1220 OE1 GLU 218 64.001 4.706 11.543 1.00 29.38 ATOM 1221 OE2 GLU 218 64.949 3.977 9.718 1.00 38.81 ATOM 1222 C GLU 218 63.794 -0.646 11.850 1.00 17.19 ATOM 1223 O GLU 218 64.669 -0.990 12.608 1.00 25.19 ATOM 1224 N TRP 219 62.514 -0.735 12.168 1.00 13.68 ATOM 1225 CA TRP 219 62.078 -1.230 13.452 1.00 11.22 ATOM 1226 CB TRP 219 60.638 -0.816 13.740 1.00 15.63 ATOM 1227 CG TRP 219 60.475 0.563 14.192 1.00 19.27 ATOM 1228 CD2 TRP 219 59.249 1.297 14.263 1.00 17.84 ATOM 1229 CE2 TRP 219 59.555 2.568 14.791 1.00 16.01 ATOM 1230 CE3 TRP 219 57.918 1.000 13.924 1.00 22.82 ATOM 1231 CD1 TRP 219 61.450 1.395 14.658 1.00 20.82 ATOM 1232 NE1 TRP 219 60.903 2.600 15.021 1.00 21.26 ATOM 1233 CZ2 TRP 219 58.589 3.547 14.992 1.00 17.84 ATOM 1234 CZ3 TRP 219 56.945 1.982 14.121 1.00 20.61 ATOM 1235 CH2 TRP 219 57.289 3.238 14.651 1.00 24.23 ATOM 1236 C TRP 219 62.093 -2.729 13.468 1.00 12.69 ATOM 1237 O TRP 219 61.905 -3.326 14.498 1.00 20.36 ATOM 1238 N GLY 220 62.215 -3.370 12.331 1.00 14.83 ATOM 1239 CA GLY 220 62.209 -4.816 12.384 1.00 15.91 ATOM 1240 C GLY 220 60.923 -5.447 11.862 1.00 19.27 ATOM 1241 O GLY 220 60.858 -6.662 11.767 1.00 23.97 ATOM 1242 N TYR 221 59.884 -4.679 11.563 1.00 13.12 ATOM 1243 CA TYR 221 58.684 -5.297 11.010 1.00 15.79 ATOM 1244 CB TYR 221 57.579 -4.281 10.897 1.00 14.40 ATOM 1245 CG TYR 221 56.915 -3.953 12.186 1.00 13.85 ATOM 1246 CD1 TYR 221 56.823 -2.645 12.607 1.00 15.85 ATOM 1247 CE1 TYR 221 56.110 -2.315 13.725 1.00 17.59 ATOM 1248 CD2 TYR 221 56.283 -4.941 12.939 1.00 13.29 ATOM 1249 CE2 TYR 221 55.564 -4.623 14.063 1.00 14.03 ATOM 1250 CZ TYR 221 55.489 -3.301 14.443 1.00 16.10 ATOM 1251 OH TYR 221 54.791 -2.942 15.554 1.00 26.08 ATOM 1252 C TYR 221 58.972 -5.817 9.595 1.00 20.08 ATOM 1253 O TYR 221 59.828 -5.291 8.905 1.00 25.54 ATOM 1254 N SER 222 58.253 -6.832 9.140 1.00 22.90 ATOM 1255 CA SER 222 58.481 -7.354 7.790 1.00 25.01 ATOM 1256 CB SER 222 58.412 -8.881 7.807 1.00 25.19 ATOM 1257 OG SER 222 57.154 -9.300 8.332 1.00 30.91 ATOM 1258 C SER 222 57.437 -6.787 6.818 1.00 23.30 ATOM 1259 O SER 222 56.534 -6.062 7.241 1.00 24.16 ATOM 1260 N SER 223 57.542 -7.159 5.539 1.00 24.20 ATOM 1261 CA SER 223 56.613 -6.7.05 4.486 1.00 22.69 ATOM 1262 CB SER 223 56.827 -7.473 3.162 1.00 25.01 ATOM 1263 OG SER 223 57.699 -6.777 2.293 1.00 30.78 ATOM 1264 C SER 223 55.178 -6.882 4.910 1.00 18.96 ATOM 1265 O SER 223 54.408 -5.924 4.904 1.00 24.83 ATOM 1266 N GLU 224 54.849 -8.100 5.331 1.00 14.34 ATOM 1267 CA GLU 224 53.510 -8.430 5.768 1.00 14.70 ATOM 1268 CB GLU 224 53.452 -9.881 6.241 1.00 11.94 ATOM 1269 CG GLU 224 53.594 -10.917 5.139 1.00 6.62 ATOM 1270 CD GLU 224 55.008 -11.084 4.574 1.00 11.92 ATOM 1271 OE1 GLU 224 56.032 -10.939 5.277 1.00 17.07 ATOM 1272 OE2 GLU 224 55.100 -11.431 3.392 1.00 19.14 ATOM 1273 C GLU 224 53.020 -7.494 6.860 1.00 16.93 ATOM 1274 O GLU 224 51.982 -6.859 6.719 1.00 23.58 ATOM 1275 N ASP 225 53.794 -7.368 7.928 1.00 21.13 ATOM 1276 CA ASP 225 53.423 -6.518 9.037 1.00 14.44 ATOM 1277 CB ASP 225 54.554 -6.451 10.050 1.00 20.30 ATOM 1278 CG ASP 225 54.686 -7.712 10.863 1.00 22.22 ATOM 1279 OD1 ASP 225 53.700 -8.071 11.531 1.00 22.32 ATOM 1280 OD2 ASP 225 55.782 -8.315 10.861 1.00 18.56 ATOM 1281 C ASP 225 53.156 -5.127 8.534 1.00 19.11 ATOM 1282 O ASP 225 52.081 -4.583 8.761 1.00 22.45 ATOM 1283 N VAL 226 54.130 -4.547 7.843 1.00 17.57 ATOM 1284 CA VAL 226 53.972 -3.206 7.332 1.00 18.36 ATOM 1285 CB VAL 226 55.266 -2.702 6.681 1.00 17.30 ATOM 1286 CG1 VAL 226 55.029 -1.374 6.029 1.00 16.11 ATOM 1287 CG2 VAL 226 56.345 -2.540 7.739 1.00 16.32 ATOM 1288 C VAL 226 52.762 -3.050 6.392 1.00 20.92 ATOM 1289 O VAL 226 52.072 -2.031 6.467 1.00 24.32 ATOM 1290 N ALA 227 52.472 -4.051 5.551 1.00 19.82 ATOM 1291 CA ALA 227 51.314 -3.986 4.634 1.00 19.35 ATOM 1292 CB ALA 227 51.397 -5.063 3.574 1.00 15.70 ATOM 1293 C ALA 227 49.962 -4.081 5.380 1.00 19.98 ATOM 1294 O ALA 227 48.943 -3.530 4.945 1.00 21.24 ATOM 1295 N GLU 228 49.947 -4.797 6.493 1.00 16.52 ATOM 1296 CA GLU 228 48.735 -4.905 7.275 1.00 15.88 ATOM 1297 CB GLU 228 48.932 -5.920 8.395 1.00 18.82 ATOM 1298 CG GLU 228 48.725 -7.341 7.906 1.00 23.82 ATOM 1299 CD GLU 228 49.723 -8.330 8.473 1.00 28.53 ATOM 1300 OE1 GLU 228 50.241 -9.159 7.694 1.00 30.67 ATOM 1301 OE2 GLU 228 49.979 -8.296 9.692 1.00 32.83 ATOM 1302 C GLU 228 48.381 -3.535 7.812 1.00 12.58 ATOM 1303 O GLU 228 47.222 -3.150 7.817 1.00 15.95 ATOM 1304 N PHE 229 49.398 -2.785 8.222 1.00 13.17 ATOM 1305 CA PHE 229 49.207 -1.438 8.730 1.00 13.77 ATOM 1306 CB PHE 229 50.512 -0.911 9.340 1.00 13.96 ATOM 1307 CG PHE 229 50.856 -1.526 10.682 1.00 12.34 ATOM 1308 CD1 PHE 229 52.140 -2.010 10.944 1.00 12.39 ATOM 1309 CD2 PHE 229 49.890 -1.636 11.686 1.00 12.04 ATOM 1310 CE1 PHE 229 52.454 -2.597 12.171 1.00 8.60 ATOM 1311 CE2 PHE 229 50.207 -2.224 12.928 1.00 9.34 ATOM 1312 CZ PHE 229 51.479 -2.701 13.164 1.00 6.27 ATOM 1313 C PHE 229 48.698 -0.501 7.623 1.00 16.58 ATOM 1314 O PHE 229 47.732 0.240 7.829 1.00 17.11 ATOM 1315 N TYR 230 49.321 -0.545 6.443 1.00 17.83 ATOM 1316 CA TYR 230 48.889 0.306 5.308 1.00 18.63 ATOM 1317 CB TYR 230 49.775 0.095 4.085 1.00 17.05 ATOM 1318 CG TYR 230 49.660 1.160 3.027 1.00 19.90 ATOM 1319 CD1 TYR 230 50.175 2.435 3.245 1.00 20.56 ATOM 1320 CE1 TYR 230 50.141 3.410 2.266 1.00 17.60 ATOM 1321 CD2 TYR 230 49.092 0.887 1.786 1.00 20.54 ATOM 1322 CE2 TYR 230 49.048 1.858 0.798 1.00 21.92 ATOM 1323 CZ TYR 230 49.583 3.121 1.047 1.00 24.08 ATOM 1324 OH TYR 230 49.569 4.100 0.079 1.00 22.12 ATOM 1325 C TYR 230 47.452 -0.014 4.941 1.00 14.05 ATOM 1326 O TYR 230 46.630 0.873 4.867 1.00 18.48 ATOM 1327 N HIS 231 47.152 -1.288 4.724 1.00 15.20 ATOM 1328 CA HIS 231 45.789 -1.698 4.408 1.00 16.34 ATOM 1329 CB HIS 231 45.657 -3.218 4.400 1.00 19.85 ATOM 1330 CG HIS 231 46.101 -3.869 3.126 1.00 27.74 ATOM 1331 CD2 HIS 231 47.267 -3.787 2.433 1.00 30.71 ATOM 1332 ND1 HIS 231 45.308 -4.754 2.423 1.00 28.38 ATOM 1333 CE1 HIS 231 45.963 -5.185 1.361 1.00 29.98 ATOM 1334 NE2 HIS 231 47.155 -4.612 1.343 1.00 22.31 ATOM 1335 C HIS 231 44.846 -1.125 5.466 1.00 18.40 ATOM 1336 O HIS 231 43.840 -0.507 5.141 1.00 27.16 ATOM 1337 N ARG 232 45.192 -1.281 6.735 1.00 18.07 ATOM 1338 CA ARG 232 44.354 -0.766 7.806 1.00 15.74 ATOM 1339 CB ARG 232 44.940 -1.137 9.171 1.00 22.99 ATOM 1340 CG ARG 232 44.049 -0.764 10.379 1.00 22.30 ATOM 1341 CD ARG 232 44.601 -1.380 11.641 1.00 25.70 ATOM 1342 NE ARG 232 44.646 -2.838 11.520 1.00 33.18 ATOM 1343 CZ ARG 232 45.690 -3.613 11.826 1.00 33.26 ATOM 1344 NH1 ARG 232 46.835 -3.093 12.292 1.00 22.03 ATOM 1345 NH2 ARG 232 45.572 -4.932 11.658 1.00 35.05 ATOM 1346 C ARG 232 44.202 0.738 7.727 1.00 17.28 ATOM 1347 O ARG 232 43.099 1.246 7.931 1.00 15.75 ATOM 1348 N GLN 233 45.300 1.448 7.431 1.00 16.95 ATOM 1349 CA GLN 233 45.272 2.903 7.343 1.00 10.93 ATOM 1350 CB GLN 233 46.656 3.455 7.062 1.00 12.92 ATOM 1351 CG GLN 233 46.688 4.957 6.820 1.00 7.74 ATOM 1352 CD GLN 233 48.094 5.498 6.787 1.00 9.89 ATOM 1353 OE1 GLN 233 49.047 4.762 6.991 1.00 7.65 ATOM 1354 NE2 GLN 233 48.227 6.795 6.603 1.00 10.54 ATOM 1355 C GLN 233 44.310 3.360 6.264 1.00 15.42 ATOM 1356 O GLN 233 43.520 4.295 6.480 1.00 17.48 ATOM 1357 N LEU 234 44.360 2.707 5.104 1.00 11.75 ATOM 1358 CA LEU 234 43.467 3.080 4.018 1.00 11.38 ATOM 1359 CB LEU 234 43.788 2.276 2.753 1.00 15.07 ATOM 1360 CG LEU 234 45.197 2.340 2.165 1.00 16.15 ATOM 1361 CD1 LEU 234 45.214 1.734 0.753 1.00 16.02 ATOM 1362 CD2 LEU 234 45.639 3.778 2.121 1.00 15.26 ATOM 1363 C LEU 234 42.003 2.849 4.420 1.00 12.48 ATOM 1364 O LEU 234 41.157 3.716 4.243 1.00 19.53 ATOM 1365 N LYS 235 41.727 1.681 4.982 1.00 13.76 ATOM 1366 CA LYS 235 40.396 1.277 5.413 1.00 15.08 ATOM 1367 CB LYS 235 40.483 -0.131 5.970 1.00 20.96 ATOM 1368 CG LYS 235 39.259 -0.982 5.768 1.00 30.47 ATOM 1369 CD LYS 235 39.452 -2.367 6.394 1.00 40.95 ATOM 1370 CE LYS 235 40.776 -3.043 5.947 1.00 49.89 ATOM 1371 NZ LYS 235 41.705 -3.351 7.117 1.00 50.92 ATOM 1372 C LYS 235 39.802 2.186 6.470 1.00 18.56 ATOM 1373 O LYS 235 38.613 2.442 6.462 1.00 22.95 ATOM 1374 N LEU 236 40.619 2.649 7.410 1.00 21.51 ATOM 1375 CA LEU 236 40.134 3.538 8.462 1.00 14.99 ATOM 1376 CB LEU 236 41.000 3.415 9.708 1.00 19.28 ATOM 1377 CG LEU 236 40.947 1.987 10.248 1.00 17.90 ATOM 1378 CD1 LEU 236 41.728 1.889 11.495 1.00 22.07 ATOM 1379 CD2 LEU 236 39.531 1.624 10.530 1.00 21.26 ATOM 1380 C LEU 236 40.028 4.981 8.019 1.00 17.01 ATOM 1381 O LEU 236 39.148 5.701 8.477 1.00 20.51 ATOM 1382 N THR 237 40.907 5.427 7.129 1.00 16.17 ATOM 1383 CA THR 237 40.808 6.803 6.642 1.00 15.50 ATOM 1384 CB THR 237 41.824 7.070 5.543 1.00 15.39 ATOM 1385 OG1 THR 237 43.144 6.962 6.077 1.00 17.24 ATOM 1386 CG2 THR 237 41.627 8.446 4.968 1.00 16.40 ATOM 1387 C THR 237 39.414 6.972 6.028 1.00 20.09 ATOM 1388 O THR 237 38.776 8.002 6.162 1.00 20.01 ATOM 1389 N GLN 238 38.960 5.933 5.343 1.00 23.44 ATOM 1390 CA GLN 238 37.670 5.948 4.714 1.00 24.58 ATOM 1391 CB GLN 238 37.559 4.775 3.738 1.00 24.07 ATOM 1392 CG GLN 238 36.197 4.628 3.068 1.00 28.51 ATOM 1393 CD GLN 238 35.322 3.583 3.724 1.00 31.81 ATOM 1394 OE1 GLN 238 34.185 3.857 4.136 1.00 34.84 ATOM 1395 NE2 GLN 238 35.840 2.367 3.816 1.00 34.59 ATOM 1396 C GLN 238 36.614 5.861 5.801 1.00 26.68 ATOM 1397 O GLN 238 35.709 6.685 5.855 1.00 28.24 ATOM 1398 N GLN 239 36.750 4.889 6.693 1.00 28.41 ATOM 1399 CA GLN 239 35.777 4.718 7.768 1.00 26.98 ATOM 1400 CB GLN 239 36.138 3.536 8.644 1.00 34.27 ATOM 1401 CG GLN 239 35.788 2.203 8.062 1.00 42.96 ATOM 1402 CD GLN 239 35.792 1.116 9.118 1.00 51.22 ATOM 1403 OE1 GLN 239 35.586 1.383 10.318 1.00 51.30 ATOM 1404 NE2 GLN 239 36.012 -0.118 8.685 1.00 54.93 ATOM 1405 C GLN 239 35.585 5.933 8.644 1.00 22.08 ATOM 1406 O GLN 239 34.460 6.397 8.793 1.00 24.27 ATOM 1407 N TYR 240 36.669 6.420 9.257 1.00 22.64 ATOM 1408 CA TYR 240 36.626 7.607 10.139 1.00 20.71 ATOM 1409 CB TYR 240 38.010 7.923 10.729 1.00 16.77 ATOM 1410 CG TYR 240 38.618 6.840 11.637 1.00 17.42 ATOM 1411 CD1 TYR 240 37.821 6.001 12.432 1.00 17.36 ATOM 1412 CE1 TYR 240 38.400 5.024 13.262 1.00 17.77 ATOM 1413 CD2 TYR 240 40.004 6.667 11.703 1.00 19.31 ATOM 1414 CE2 TYR 240 40.585 5.698 12.525 1.00 19.41 ATOM 1415 CZ TYR 240 39.781 4.881 13.295 1.00 19.35 ATOM 1416 OH TYR 240 40.373 3.879 14.031 1.00 19.37 ATOM 1417 C TYR 240 36.038 8.858 9.463 1.00 19.71 ATOM 1418 O TYR 240 35.248 9.588 10.077 1.00 18.91 ATOM 1419 N THR 241 36.422 9.082 8.205 1.00 20.29 ATOM 1420 CA THR 241 35.938 10.195 7.397 1.00 16.59 ATOM 1421 CB THR 241 36.619 10.194 5.995 1.00 21.67 ATOM 1422 OG1 THR 241 38.003 10.546 6.133 1.00 19.88 ATOM 1423 CG2 THR 241 35.923 11.168 4.990 1.00 20.34 ATOM 1424 C THR 241 34.427 10.065 7.222 1.00 16.73 ATOM 1425 O THR 241 33.672 10.988 7.536 1.00 20.54 ATOM 1426 N ASP 242 33.982 8.916 6.734 1.00 17.09 ATOM 1427 CA ASP 242 32.563 8.690 6.533 1.00 21.69 ATOM 1428 CB ASP 242 32.299 7.300 5.954 1.00 21.39 ATOM 1429 CG ASP 242 32.603 7.197 4.465 1.00 20.65 ATOM 1430 OD1 ASP 242 32.855 8.232 3.813 1.00 18.80 ATOM 1431 OD2 ASP 242 32.575 6.058 3.951 1.00 19.59 ATOM 1432 C ASP 242 31.790 8.839 7.847 1.00 25.51 ATOM 1433 O ASP 242 30.699 9.423 7.855 1.00 28.83 ATOM 1434 N HIS 243 32.344 8.354 8.961 1.00 21.95 ATOM 1435 CA HIS 243 31.615 8.463 10.220 1.00 18.92 ATOM 1436 CB HIS 243 32.309 7.708 11.352 1.00 17.61 ATOM 1437 CG HIS 243 31.690 7.935 12.700 1.00 12.62 ATOM 1438 CD2 HIS 243 31.795 8.970 13.562 1.00 14.95 ATOM 1439 ND1 HIS 243 30.935 6.981 13.349 1.00 16.29 ATOM 1440 CE1 HIS 243 30.620 7.411 14.557 1.00 9.95 ATOM 1441 NE2 HIS 243 31.130 8.616 14.709 1.00 16.91 ATOM 1442 C HIS 243 31.383 9.904 10.628 1.00 21.10 ATOM 1443 O HIS 243 30.301 10.249 11.070 1.00 25.20 ATOM 1444 N CYS 244 32.413 10.734 10.539 1.00 20.17 ATOM 1445 CA CYS 244 32.271 12.128 10.916 1.00 20.48 ATOM 1446 CB CYS 244 33.624 12.819 10.883 1.00 18.34 ATOM 1447 SG CYS 244 34.760 12.105 12.050 1.00 16.47 ATOM 1448 C CYS 244 31.269 12.890 10.058 1.00 21.21 ATOM 1449 O CYS 244 30.462 13.654 10.576 1.00 22.28 ATOM 1450 N VAL 245 31.312 12.683 8.746 1.00 22.25 ATOM 1451 CA VAL 245 30.395 13.376 7.841 1.00 22.33 ATOM 1452 CB VAL 245 30.781 13.140 6.359 1.00 19.36 ATOM 1453 CG1 VAL 245 29.816 13.827 5.446 1.00 21.10 ATOM 1454 CG2 VAL 245 32.171 13.691 6.093 1.00 17.45 ATOM 1455 C VAL 245 28.957 12.942 8.118 1.00 21.40 ATOM 1456 O VAL 245 28.055 13.770 8.214 1.00 22.33 ATOM 1457 N ASN 246 28.780 11.651 8.348 1.00 21.90 ATOM 1458 CA ASN 246 27.477 11.063 8.620 1.00 23.19 ATOM 1459 CB ASN 246 27.639 9.557 8.771 1.00 34.68 ATOM 1460 CG ASN 246 26.366 8.855 9.237 1.00 44.33 ATOM 1461 OD1 ASN 246 25.741 9.220 10.248 1.00 48.73 ATOM 1462 ND2 ASN 246 26.015 7.790 8.530 1.00 50.65 ATOM 1463 C ASN 246 26.790 11.631 9.854 1.00 22.82 ATOM 1464 O ASN 246 25.626 12.038 9.797 1.00 24.79 ATOM 1465 N TRP 247 27.487 11.615 10.981 1.00 20.19 ATOM 1466 CA TRP 247 26.906 12.120 12.208 1.00 18.58 ATOM 1467 CB TRP 247 27.694 11.620 13.418 1.00 17.89 ATOM 1468 CG TRP 247 27.467 10.185 13.549 1.00 21.14 ATOM 1469 CD2 TRP 247 26.199 9.532 13.782 1.00 22.32 ATOM 1470 CE2 TRP 247 26.388 8.158 13.537 1.00 22.60 ATOM 1471 CE3 TRP 247 24.920 9.982 14.167 1.00 22.25 ATOM 1472 CD1 TRP 247 28.337 9.210 13.222 1.00 23.88 ATOM 1473 NE1 TRP 247 27.701 7.991 13.194 1.00 25.03 ATOM 1474 CZ2 TRP 247 25.348 7.214 13.659 1.00 22.59 ATOM 1475 CZ3 TRP 247 23.883 9.045 14.289 1.00 15.92 ATOM 1476 CH2 TRP 247 24.107 7.679 14.036 1.00 21.52 ATOM 1477 C TRP 247 26.734 13.619 12.203 1.00 21.26 ATOM 1478 O TRP 247 25.872 14.151 12.888 1.00 23.07 ATOM 1479 N TYR 248 27.530 14.291 11.385 1.00 22.21 ATOM 1480 CA TYR 248 27.469 15.733 11.270 1.00 19.44 ATOM 1481 CB TYR 248 28.634 16.262 10.397 1.00 22.06 ATOM 1482 CG TYR 248 28.500 17.715 9.992 1.00 15.39 ATOM 1483 CD1 TYR 248 28.656 18.733 10.924 1.00 18.30 ATOM 1484 CE1 TYR 248 28.429 20.049 10.589 1.00 19.55 ATOM 1485 CD2 TYR 248 28.120 18.059 8.700 1.00 17.91 ATOM 1486 CE2 TYR 248 27.883 19.376 8.354 1.00 15.27 ATOM 1487 CZ TYR 248 28.037 20.369 9.299 1.00 17.78 ATOM 1488 OH TYR 248 27.793 21.684 8.965 1.00 25.83 ATOM 1489 C TYR 248 26.158 16.041 10.611 1.00 20.61 ATOM 1490 O TYR 248 25.378 16.842 11.111 1.00 22.05 ATOM 1491 N ASN 249 25.892 15.369 9.500 1.00 23.02 ATOM 1492 CA ASN 249 24.664 15.626 8.778 1.00 23.67 ATOM 1493 CB ASN 249 24.597 14.835 7.483 1.00 21.11 ATOM 1494 CG ASN 249 25.513 15.393 6.422 1.00 22.16 ATOM 1495 OD1 ASN 249 25.870 16.560 6.461 1.00 29.65 ATOM 1496 ND2 ASN 249 25.918 14.556 5.478 1.00 23.60 ATOM 1497 C ASN 249 23.490 15.315 9.655 1.00 25.98 ATOM 1498 O ASN 249 22.552 16.119 9.737 1.00 28.81 ATOM 1499 N VAL 250 23.581 14.197 10.378 1.00 25.43 ATOM 1500 CA VAL 250 22.507 13.792 11.270 1.00 23.20 ATOM 1501 CB VAL 250 22.777 12.430 11.913 1.00 22.17 ATOM 1502 CG1 VAL 250 21.826 12.188 13.069 1.00 17.43 ATOM 1503 CG2 VAL 250 22.594 11.343 10.894 1.00 18.80 ATOM 1504 C VAL 250 22.247 14.833 12.345 1.00 25.76 ATOM 1505 O VAL 250 21.101 15.166 12.599 1.00 34.35 ATOM 1506 N GLY 251 23.292 15.373 12.955 1.00 24.96 ATOM 1507 CA GLY 251 23.092 16.373 13.986 1.00 23.97 ATOM 1508 C GLY 251 22.657 17.701 13.402 1.00 28.06 ATOM 1509 O GLY 251 21.793 18.396 13.947 1.00 31.01 ATOM 1510 N LEU 252 23.273 18.070 12.290 1.00 29.10 ATOM 1511 CA LEU 252 22.957 19.321 11.628 1.00 28.66 ATOM 1512 CB LEU 252 23.704 19.424 10.309 1.00 23.77 ATOM 1513 CG LEU 252 23.320 20.699 9.575 1.00 22.56 ATOM 1514 CD1 LEU 252 23.869 21.892 10.323 1.00 26.59 ATOM 1515 CD2 LEU 252 23.816 20.672 8.152 1.00 24.48 ATOM 1516 C LEU 252 21.474 19.391 11.342 1.00 30.41 ATOM 1517 O LEU 252 20.801 20.344 11.716 1.00 32.91 ATOM 1518 N ASN 253 20.966 18.347 10.711 1.00 30.60 ATOM 1519 CA ASN 253 19.569 18.295 10.351 1.00 33.65 ATOM 1520 CB ASN 253 19.316 17.160 9.372 1.00 35.63 ATOM 1521 CG ASN 253 19.862 17.463 7.994 1.00 42.54 ATOM 1522 OD1 ASN 253 20.855 18.186 7.835 1.00 42.40 ATOM 1523 ND2 ASN 253 19.203 16.930 6.981 1.00 50.55 ATOM 1524 C ASN 253 18.599 18.235 11.507 1.00 33.58 ATOM 1525 O ASN 253 17.414 18.515 11.336 1.00 37.79 ATOM 1526 N GLY 254 19.085 17.900 12.693 1.00 31.74 ATOM 1527 CA GLY 254 18.189 17.842 13.839 1.00 29.82 ATOM 1528 C GLY 254 17.844 19.241 14.310 1.00 29.07 ATOM 1529 O GLY 254 16.876 19.454 15.024 1.00 29.77 ATOM 1530 N LEU 255 18.645 20.208 13.885 1.00 28.00 ATOM 1531 CA LEU 255 18.448 21.586 14.269 1.00 26.04 ATOM 1532 CB LEU 255 19.804 22.200 14.577 1.00 22.14 ATOM 1533 CG LEU 255 20.563 21.304 15.563 1.00 27.96 ATOM 1534 CD1 LEU 255 22.068 21.563 15.626 1.00 26.56 ATOM 1535 CD2 LEU 255 19.938 21.483 16.905 1.00 27.86 ATOM 1536 C LEU 255 17.687 22.391 13.209 1.00 30.33 ATOM 1537 O LEU 255 17.556 23.608 13.330 1.00 35.36 ATOM 1538 N ARG 256 17.187 21.726 12.169 1.00 31.16 ATOM 1539 CA ARG 256 16.436 22.438 11.145 1.00 32.82 ATOM 1540 CB ARG 256 16.244 21.610 9.865 1.00 31.47 ATOM 1541 CG ARG 256 17.508 21.568 9.000 1.00 35.00 ATOM 1542 CD ARG 256 17.291 21.321 7.501 1.00 30.02 ATOM 1543 NE ARG 256 18.344 22.019 6.759 1.00 34.65 ATOM 1544 CZ ARG 256 19.515 21.489 6.394 1.00 40.31 ATOM 1545 NH1 ARG 256 20.404 22.236 5.758 1.00 47.05 ATOM 1546 NH2 ARG 256 19.788 20.205 6.587 1.00 44.05 ATOM 1547 C ARG 256 15.106 22.738 11.775 1.00 36.39 ATOM 1548 O ARG 256 14.455 21.844 12.325 1.00 39.88 ATOM 1549 N GLY 257 14.772 24.020 11.792 1.00 37.32 ATOM 1550 CA GLY 257 13.522 24.492 12.359 1.00 37.66 ATOM 1551 C GLY 257 13.120 25.647 11.475 1.00 39.38 ATOM 1552 O GLY 257 13.795 25.892 10.466 1.00 45.14 ATOM 1553 N SER 258 12.069 26.377 11.830 1.00 39.54 ATOM 1554 CA SER 258 11.625 27.496 10.989 1.00 40.17 ATOM 1555 CB SER 258 10.131 27.380 10.721 1.00 39.14 ATOM 1556 OG SER 258 9.461 27.094 11.930 1.00 43.54 ATOM 1557 C SER 258 11.921 28.885 11.518 1.00 37.11 ATOM 1558 O SER 258 11.872 29.862 10.779 1.00 35.66 ATOM 1559 N THR 259 12.259 28.957 12.790 1.00 37.79 ATOM 1560 CA THR 259 12.518 30.215 13.455 1.00 41.44 ATOM 1561 CB THR 259 12.301 30.043 14.951 1.00 45.91 ATOM 1562 OG1 THR 259 11.504 28.874 15.180 1.00 55.55 ATOM 1563 CG2 THR 259 11.600 31.273 15.530 1.00 55.48 ATOM 1564 C THR 259 13.899 30.826 13.285 1.00 38.35 ATOM 1565 O THR 259 14.813 30.213 12.739 1.00 41.82 ATOM 1566 N TYR 260 14.020 32.057 13.771 1.00 35.05 ATOM 1567 CA TYR 260 15.269 32.786 13.777 1.00 31.66 ATOM 1568 CB TYR 260 15.049 34.194 14.305 1.00 26.91 ATOM 1569 CG TYR 260 16.340 34.934 14.460 1.00 26.27 ATOM 1570 CD1 TYR 260 16.998 35.438 13.349 1.00 28.25 ATOM 1571 CE1 TYR 260 18.205 36.077 13.463 1.00 26.96 ATOM 1572 CD2 TYR 260 16.933 35.097 15.702 1.00 28.45 ATOM 1573 CE2 TYR 260 18.152 35.740 15.828 1.00 26.78 ATOM 1574 CZ TYR 260 18.770 36.224 14.696 1.00 27.71 ATOM 1575 OH TYR 260 19.957 36.878 14.774 1.00 36.80 ATOM 1576 C TYR 260 16.160 32.065 14.773 1.00 34.78 ATOM 1577 O TYR 260 17.357 31.917 14.557 1.00 37.21 ATOM 1578 N ASP 261 15.566 31.656 15.891 1.00 37.42 ATOM 1579 CA ASP 261 16.295 30.961 16.942 1.00 40.44 ATOM 1580 CB ASP 261 15.413 30.745 18.165 1.00 46.19 ATOM 1581 CG ASP 261 16.204 30.322 19.386 1.00 52.07 ATOM 1582 OD1 ASP 261 17.336 30.836 19.573 1.00 55.53 ATOM 1583 OD2 ASP 261 15.692 29.482 20.159 1.00 54.28 ATOM 1584 C ASP 261 16.734 29.626 16.411 1.00 40.15 ATOM 1585 O ASP 261 17.863 29.195 16.644 1.00 40.37 ATOM 1586 N ALA 262 15.823 28.974 15.697 1.00 40.43 ATOM 1587 CA ALA 262 16.113 27.679 15.104 1.00 39.06 ATOM 1588 CB ALA 262 14.936 27.183 14.297 1.00 36.99 ATOM 1589 C ALA 262 17.324 27.863 14.209 1.00 38.56 ATOM 1590 O ALA 262 18.222 27.031 14.213 1.00 42.67 ATOM 1591 N TRP 263 17.372 28.972 13.475 1.00 34.48 ATOM 1592 CA TRP 263 18.501 29.200 12.612 1.00 30.51 ATOM 1593 CB TRP 263 18.254 30.341 11.647 1.00 29.10 ATOM 1594 CG TRP 263 19.279 30.344 10.580 1.00 27.55 ATOM 1595 CD2 TRP 263 20.493 31.087 10.566 1.00 26.16 ATOM 1596 CE2 TRP 263 21.195 30.722 9.389 1.00 27.70 ATOM 1597 CE3 TRP 263 21.063 32.022 11.434 1.00 25.40 ATOM 1598 CD1 TRP 263 19.281 29.586 9.447 1.00 30.08 ATOM 1599 NE1 TRP 263 20.429 29.803 8.727 1.00 25.78 ATOM 1600 CZ2 TRP 263 22.441 31.264 9.050 1.00 26.88 ATOM 1601 CZ3 TRP 263 22.307 32.565 11.105 1.00 32.51 ATOM 1602 CH2 TRP 263 22.986 32.178 9.912 1.00 33.60 ATOM 1603 C TRP 263 19.800 29.438 13.373 1.00 31.82 ATOM 1604 O TRP 263 20.761 28.703 13.176 1.00 33.27 ATOM 1605 N VAL 264 19.838 30.415 14.269 1.00 29.96 ATOM 1606 CA VAL 264 21.088 30.704 14.981 1.00 33.08 ATOM 1607 CB VAL 264 20.955 31.885 15.992 1.00 35.92 ATOM 1608 CG1 VAL 264 20.488 33.142 15.272 1.00 35.34 ATOM 1609 CG2 VAL 264 19.991 31.534 17.130 1.00 40.92 ATOM 1610 C VAL 264 21.726 29.488 15.651 1.00 33.22 ATOM 1611 O VAL 264 22.948 29.417 15.762 1.00 33.90 ATOM 1612 N LYS 265 20.907 28.521 16.059 1.00 33.23 ATOM 1613 CA LYS 265 21.414 27.303 16.697 1.00 34.85 ATOM 1614 CB LYS 265 20.343 26.643 17.564 1.00 37.37 ATOM 1615 CG LYS 265 20.023 27.416 18.819 1.00 44.29 ATOM 1616 CD LYS 265 19.068 26.626 19.676 1.00 55.75 ATOM 1617 CE LYS 265 18.503 27.475 20.813 1.00 63.56 ATOM 1618 NZ LYS 265 17.404 26.772 21.560 1.00 68.84 ATOM 1619 C LYS 265 21.912 26.317 15.652 1.00 32.74 ATOM 1620 O LYS 265 22.906 25.631 15.855 1.00 31.29 ATOM 1621 N PHE 266 21.189 26.259 14.545 1.00 30.50 ATOM 1622 CA PHE 266 21.515 25.422 13.411 1.00 27.65 ATOM 1623 CB PHE 266 20.411 25.601 12.373 1.00 23.05 ATOM 1624 CG PHE 266 20.742 25.066 11.028 1.00 26.10 ATOM 1625 CD1 PHE 266 20.494 23.727 10.714 1.00 23.77 ATOM 1626 CD2 PHE 266 21.253 25.915 16.036 1.00 27.75 ATOM 1627 CE1 PHE 266 20.746 23.235 9.426 1.00 20.79 ATOM 1628 CE2 PHE 266 21.506 25.434 8.748 1.00 25.12 ATOM 1629 CZ PHE 266 21.247 24.079 8.447 1.00 20.14 ATOM 1630 C PHE 266 22.868 25.865 12.843 1.00 28.95 ATOM 1631 O PHE 266 23.705 25.034 12.494 1.00 33.21 ATOM 1632 N ASN 267 23.080 27.177 12.769 1.00 27.02 ATOM 1633 CA ASN 267 24.323 27.716 12.244 1.00 26.43 ATOM 1634 CB ASN 267 24.175 29.175 11.812 1.00 25.78 ATOM 1635 CG ASN 267 25.484 29.752 11.261 1.00 30.92 ATOM 1636 OD1 ASN 267 25.979 29.315 10.216 1.00 34.66 ATOM 1637 ND2 ASN 267 26.061 30.707 11.975 1.00 31.20 ATOM 1638 C ASN 267 25.497 27.609 13.197 1.00 28.55 ATOM 1639 O ASN 267 26.640 27.638 12.760 1.00 35.77 ATOM 1640 N ARG 268 25.246 27.537 14.498 1.00 30.56 ATOM 1641 CA ARG 268 26.345 27.433 15.452 1.00 26.63 ATOM 1642 CB ARG 268 25.851 27.773 16.844 1.00 31.27 ATOM 1643 CG ARG 268 26.959 28.125 17.764 1.00 42.83 ATOM 1644 CD ARG 268 26.452 28.417 19.139 1.00 52.31 ATOM 1645 NE ARG 268 27.563 28.446 20.076 1.00 61.73 ATOM 1646 CZ ARG 268 27.510 27.929 21.295 1.00 68.05 ATOM 1647 NH1 ARG 268 28.574 27.980 22.086 1.00 71.21 ATOM 1648 NH2 ARG 268 26.382 27.374 21.725 1.00 75.05 ATOM 1649 C ARG 268 26.955 26.028 15.407 1.00 25.08 ATOM 1650 O ARG 268 28.157 25.861 15.470 1.00 24.26 ATOM 1651 N PHE 269 26.106 25.020 15.284 1.00 21.54 ATOM 1652 CA PHE 269 26.547 23.645 15.194 1.00 20.29 ATOM 1653 CB PHE 269 25.315 22.731 15.080 1.00 17.88 ATOM 1654 CG PHE 269 25.631 21.252 14.947 1.00 23.71 ATOM 1655 CD1 PHE 269 25.620 20.419 16.063 1.00 22.41 ATOM 1656 CD2 PHE 269 25.870 20.677 13.691 1.00 25.94 ATOM 1657 CE1 PHE 269 25.838 19.062 15.937 1.00 20.65 ATOM 1658 CE2 PHE 269 26.091 19.315 13.552 1.00 17.14 ATOM 1659 CZ PHE 269 26.071 18.509 14.679 1.00 25.30 ATOM 1660 C PHE 269 27.361 23.588 13.917 1.00 22.39 ATOM 1661 O PHE 269 28.492 23.108 13.910 1.00 22.31 ATOM 1662 N ARG 270 26.794 24.133 12.841 1.00 24.10 ATOM 1663 CA ARG 270 27.461 24.132 11.547 1.00 22.53 ATOM 1664 CB ARG 270 26.638 24.864 10.482 1.00 21.20 ATOM 1665 CG ARG 270 27.412 25.170 9.196 1.00 17.05 ATOM 1666 CD ARG 270 26.472 25.476 8.036 1.00 20.10 ATOM 1667 NE ARG 270 25.772 26.749 8.190 1.00 24.43 ATOM 1668 CZ ARG 270 24.661 27.094 7.541 1.00 19.92 ATOM 1669 NH1 ARG 270 24.131 28.286 7.754 1.00 16.84 ATOM 1670 NH2 ARG 270 24.069 26.257 6.695 1.00 18.36 ATOM 1671 C ARG 270 28.839 24.730 11.667 1.00 21.46 ATOM 1672 O ARG 270 29.810 24.131 11.230 1.00 25.30 ATOM 1673 N ARG 271 28.943 25.893 12.286 1.00 24.12 ATOM 1674 CA ARG 271 30.258 26.509 12.435 1.00 27.33 ATOM 1675 CB ARG 271 30.155 27.931 13.0G5 1.00 23.38 ATOM 1676 CG ARG 271 31.492 28.628 13.101 1.00 19.25 ATOM 1677 CD ARG 271 31.372 30.006 13.673 1.00 15.09 ATOM 1678 NE ARG 271 30.776 30.008 15.006 1.00 23.57 ATOM 1679 CZ ARG 271 29.518 30.367 15.281 1.00 24.60 ATOM 1680 NH1 ARG 271 28.683 30.753 14.326 1.00 23.54 ATOM 1681 NH2 ARG 271 29.095 30.371 16.531 1.00 27.57 ATOM 1682 C ARG 271 31.177 25.654 13.306 1.00 27.87 ATOM 1683 O ARG 271 32.185 25.115 12.827 1.00 32.35 ATOM 1684 N GLU 272 30.812 25.516 14.574 1.00 25.58 ATOM 1685 CA GLU 272 31.603 24.761 15.525 1.00 23.38 ATOM 1686 CB GLU 272 30.882 24.679 16.864 1.00 21.26 ATOM 1687 CG GLU 272 30.754 26.023 17.597 1.00 24.09 ATOM 1688 CD GLU 272 30.583 25.877 19.126 1.00 28.18 ATOM 1689 OE1 GLU 272 30.578 24.731 19.638 1.00 27.43 ATOM 1690 OE2 GLU 272 30.475 26.912 19.826 1.00 22.15 ATOM 1691 C GLU 272 32.041 23.376 15.044 1.00 24.71 ATOM 1692 O GLU 272 33.213 23.038 15.171 1.00 29.53 ATOM 1693 N MET 273 31.152 22.600 14.425 1.00 24.06 ATOM 1694 CA MET 273 31.550 21.267 13.963 1.00 21.72 ATOM 1695 CB MET 273 30.346 20.369 13.702 1.00 18.83 ATOM 1696 CG MET 273 29.513 20.153 14.957 1.00 25.80 ATOM 1697 SD MET 273 30.469 19.573 16.380 1.00 26.36 ATOM 1698 CE MET 273 30.020 18.024 16.296 1.00 25.30 ATOM 1699 C MET 273 32.486 21.291 12.766 1.00 19.58 ATOM 1700 O MET 273 33.248 20.352 12.542 1.00 22.39 ATOM 1701 N THR 274 32.444 22.367 12.001 1.00 20.73 ATOM 1702 CA THR 274 33.326 22.506 10.857 1.00 20.99 ATOM 1703 CB THR 214 32.921 23.696 9.929 1.00 23.08 ATOM 1704 OG1 THR 274 31.617 23.470 9.369 1.00 16.49 ATOM 1705 CG2 THR 274 33.934 23.835 8.788 1.00 21.44 ATOM 1706 C THR 274 34.730 22.765 11.395 1.00 23.86 ATOM 1707 O THR 274 35.666 22.034 11.055 1.00 25.97 ATOM 1708 N LEU 275 34.869 23.779 12.251 1.00 21.98 ATOM 1709 CA LEU 275 36.175 24.142 12.813 1.00 20.62 ATOM 1710 CB LEU 275 36.035 25.349 13.741 1.00 17.97 ATOM 1711 CG LEU 275 35.412 26.626 13.158 1.00 20.11 ATOM 1712 CD1 LEU 275 35.130 27.603 14.269 1.00 15.23 ATOM 1713 CD2 LEU 275 36.304 27.264 12.143 1.00 15.87 ATOM 1714 C LEU 275 36.845 22.996 13.584 1.00 21.58 ATOM 1715 O LEU 275 38.058 22.839 13.539 1.00 19.28 ATOM 1716 N THR 276 36.029 22.168 14.226 1.00 21.92 ATOM 1717 CA THR 276 36.489 21.067 15.050 1.00 20.54 ATOM 1718 CB THR 276 35.589 20.941 16.302 1.00 20.03 ATOM 1719 OG1 THR 276 35.488 22.205 16.964 1.00 27.51 ATOM 1720 CG2 THR 276 36.174 19.971 17.264 1.00 27.26 ATOM 1721 C THR 276 36.545 19.692 14.413 1.00 18.29 ATOM 1722 O THR 276 37.294 18.850 14.864 1.00 24.41 ATOM 1723 N VAL 277 35.728 19.424 13.411 1.00 18.63 ATOM 1724 CA VAL 277 35.738 18.103 12.819 1.00 17.30 ATOM 1725 CB VAL 277 34.433 17.375 13.124 1.00 18.32 ATOM 1726 CG1 VAL 277 34.492 15.951 12.616 1.00 15.85 ATOM 1727 CG2 VAL 277 34.166 17.401 14.605 1.00 13.45 ATOM 1728 C VAL 277 35.974 18.079 11.313 1.00 24.98 ATOM 1729 O VAL 277 36.990 17.559 10.832 1.00 29.29 ATOM 1730 N LEU 278 35.027 18.619 10.558 1.00 26.28 ATOM 1731 CA LEU 278 35.135 18.639 9.100 1.00 23.05 ATOM 1732 CB LEU 278 33.947 19.402 8.480 1.00 19.55 ATOM 1733 CG LEU 278 32.553 18.888 8.879 1.00 22.14 ATOM 1734 CD1 LEU 278 31.469 19.721 8.211 1.00 21.08 ATOM 1735 CD2 LEU 278 32.375 17.427 8.536 1.00 13.56 ATOM 1736 C LEU 278 36.473 19.220 8.641 1.00 20.62 ATOM 1737 O LEU 278 37.100 18.691 7.731 1.00 21.36 ATOM 1738 N ASP 279 36.932 20.269 9.312 1.00 19.88 ATOM 1739 CA ASP 279 38.205 20.904 8.965 1.00 22.41 ATOM 1740 CB ASP 279 38.353 22.254 9.683 1.00 24.41 ATOM 1741 CG ASP 279 37.817 23.425 8.871 1.00 24.32 ATOM 1742 OD1 ASP 279 37.241 23.210 7.777 1.00 23.54 ATOM 1743 OD2 ASP 279 38.015 24.575 9.323 1.00 23.55 ATOM 1744 C ASP 279 39.428 20.016 9.242 1.00 23.05 ATOM 1745 O ASP 279 40.492 20.198 8.657 1.00 27.31 ATOM 1746 N LEU 280 39.263 19.032 10.113 1.00 23.67 ATOM 1747 CA LEU 280 40.345 18.116 10.453 1.00 17.85 ATOM 1748 CB LEU 280 40.188 17.700 11.908 1.00 12.01 ATOM 1749 CG LEU 280 41.302 16.835 12.494 1.00 14.79 ATOM 1750 CD1 LEU 280 42.512 17.735 12.874 1.00 14.08 ATOM 1751 CD2 LEU 280 40.761 16.090 13.692 1.00 2.29 ATOM 1752 C LEU 280 40.324 16.879 9.531 1.00 14.80 ATOM 1753 O LEU 280 41.348 16.453 9.015 1.00 14.17 ATOM 1754 N ILE 281 39.136 16.322 9.365 1.00 12.91 ATOM 1755 CA ILE 281 38.832 15.173 8.533 1.00 13.11 ATOM 1756 CB ILE 281 37.272 15.034 8.580 1.00 16.92 ATOM 1757 CG2 ILE 281 36.583 15.195 7.244 1.00 12.65 ATOM 1758 CG1 ILE 281 36.890 13.820 9.397 1.00 21.95 ATOM 1759 CD1 ILE 281 37.394 13.892 10.805 1.00 26.87 ATOM 1760 C ILE 281 39.427 15.268 7.089 1.00 18.88 ATOM 1761 O ILE 281 39.820 14.243 6.490 1.00 15.78 ATOM 1762 N VAL 282 39.530 16.494 6.555 1.00 17.36 ATOM 1763 CA VAL 282 40.089 16.771 5.209 1.00 14.13 ATOM 1764 CB VAL 282 40.002 18.262 4.876 1.00 14.53 ATOM 1765 CG1 VAL 282 40.212 18.503 3.418 1.00 14.65 ATOM 1766 CG2 VAL 282 38.751 18.844 5.403 1.00 18.35 ATOM 1767 C VAL 282 41.598 16.479 5.106 1.00 17.65 ATOM 1768 O VAL 282 42.124 16.243 4.014 1.00 17.42 ATOM 1769 N LEU 283 42.304 16.627 6.221 1.00 18.73 ATOM 1770 CA LEU 283 43.745 16.415 6.261 1.00 16.39 ATOM 1771 CB LEU 283 44.326 17.141 7.461 1.00 14.57 ATOM 1772 CG LEU 283 44.022 18.624 7.450 1.00 13.01 ATOM 1773 CD1 LEU 283 44.519 19.279 8.693 1.00 12.84 ATOM 1774 CD2 LEU 283 44.674 19.230 6.256 1.00 16.22 ATOM 1775 C LEU 283 44.170 14.953 6.301 1.00 17.30 ATOM 1776 O LEU 283 45.294 14.644 5.929 1.00 22.88 ATOM 1777 N PHE 284 43.277 14.053 6.709 1.00 15.61 ATOM 1778 CA PHE 284 43.603 12.626 6.804 1.00 15.45 ATOM 1779 CB PHE 284 42.359 11.777 7.096 1.00 14.83 ATOM 1780 CG PHE 284 41.812 11.897 8.507 1.00 18.52 ATOM 1781 CD1 PHE 284 42.400 12.723 9.451 1.00 14.14 ATOM 1782 CD2 PHE 284 40.646 11.184 8.864 1.00 16.50 ATOM 1783 CE1 PHE 284 41.825 12.837 10.714 1.00 15.64 ATOM 1784 CE2 PHE 284 40.090 11.295 10.092 1.00 7.62 ATOM 1785 CZ PHE 284 40.670 12.122 11.019 1.00 9.46 ATOM 1786 C PHE 284 44.310 12.002 5.592 1.00 18.21 ATOM 1787 O PHE 284 45.276 11.266 5.760 1.00 23.49 ATOM 1788 N PRO 285 43.851 12.276 4.352 1.00 20.88 ATOM 1789 CD PRO 285 42.694 13.049 3.863 1.00 15.13 ATOM 1790 CA PRO 285 44.556 11.644 3.225 1.00 17.86 ATOM 1791 CB PRO 285 43.763 12.122 2.008 1.00 14.52 ATOM 1792 CG PRO 285 42.390 12.350 2.575 1.00 15.75 ATOM 1793 C PRO 285 46.052 11.942 3.079 1.00 14.50 ATOM 1794 O PRO 285 46.769 11.186 2.424 1.00 14.19 ATOM 1795 N PHE 286 46.534 12.995 3.722 1.00 14.02 ATOM 1796 CA PHE 286 47.937 13.353 3.602 1.00 11.79 ATOM 1797 CB PHE 286 48.089 14.849 3.714 1.00 11.85 ATOM 1798 CG PHE 286 47.175 15.597 2.800 1.00 13.93 ATOM 1799 CD1 PHE 286 47.188 15.346 1.436 1.00 14.94 ATOM 1800 CD2 PHE 286 46.257 16.502 3.302 1.00 11.76 ATOM 1801 CE1 PHE 286 46.281 15.990 0.576 1.00 14.08 ATOM 1802 CE2 PHE 286 45.348 17.150 2.455 1.00 14.35 ATOM 1803 CZ PHE 286 45.365 16.887 1.089 1.00 13.45 ATOM 1804 C PHE 286 48.849 12.631 4.571 1.00 16.19 ATOM 1805 O PHE 286 50.038 12.936 4.670 1.00 21.52 ATOM 1806 N TYR 287 48.291 11.685 5.315 1.00 19.21 ATOM 1807 CA TYR 287 49.077 10.892 6.256 1.00 20.55 ATOM 1808 CB TYR 287 48.225 10.397 7.441 1.00 19.17 ATOM 1809 CG TYR 287 47.739 11.484 8.362 1.00 16.07 ATOM 1810 CD1 TYR 287 48.456 12.671 8.498 1.00 20.52 ATOM 1811 CE1 TYR 287 48.005 13.696 9.351 1.00 24.03 ATOM 1812 CD2 TYR 287 46.560 11.335 9.097 1.00 15.61 ATOM 1813 CE2 TYR 287 46.101 12.339 9.943 1.00 16.01 ATOM 1814 CZ TYR 287 46.820 13.517 10.064 1.00 20.29 ATOM 1815 OH TYR 287 46.359 14.558 10.833 1.00 21.44 ATOM 1816 C TYR 287 49.579 9.699 5.457 1.00 21.38 ATOM 1817 O TYR 287 50.471 8.979 5.898 1.00 23.27 ATOM 1818 N ASP 288 48.971 9.469 4.298 1.00 17.30 ATOM 1819 CA ASP 288 49.378 8.368 3.430 1.00 17.56 ATOM 1820 CB ASP 288 48.270 8.102 2.397 1.00 17.03 ATOM 1821 CG ASP 288 48.601 6.972 1.427 1.00 19.23 ATOM 1822 OD1 ASP 288 47.665 6.510 0.764 1.00 16.04 ATOM 1823 OD2 ASP 288 49.766 6.541 1.309 1.00 19.93 ATOM 1824 C ASP 288 50.666 8.884 2.774 1.00 17.17 ATOM 1825 O ASP 288 50.652 9.342 1.634 1.00 15.73 ATOM 1826 N ILE 289 51.788 8.743 3.479 1.00 18.54 ATOM 1827 CA ILE 289 53.066 9.246 3.001 1.00 18.37 ATOM 1828 CB ILE 289 54.042 9.459 4.194 1.00 19.04 ATOM 1829 CG2 ILE 289 53.428 10.472 5.175 1.00 19.10 ATOM 1830 CG1 ILE 289 54.324 8.143 4.926 1.00 12.09 ATOM 1831 CD1 ILE 289 55.331 7.259 4.239 1.00 11.61 ATOM 1832 C ILE 289 53.721 8.564 1.782 1.00 21.85 ATOM 1833 O ILE 289 54.834 8.930 1.363 1.00 23.95 ATOM 1834 N ARG 290 53.037 7.567 1.224 1.00 y9.57 ATOM 1835 CA ARG 290 53.514 6.884 0.029 1.00 18.74 ATOM 1836 CB ARG 290 53.182 5.394 0.051 1.00 17.14 ATOM 1837 CG ARG 290 54.014 4.639 1.056 1.00 23.48 ATOM 1838 CD ARG 290 53.876 3.149 0.876 1.00 34.60 ATOM 1839 NE ARG 290 54.451 2.353 1.973 1.00 46.59 ATOM 1840 CZ ARG 290 55.735 2.347 2.346 1.00 47.76 ATOM 1841 NH1 ARG 290 56.626 3.117 1.725 1.00 51.55 ATOM 1842 NH2 ARG 290 56.149 1.501 3.292 1.00 45.76 ATOM 1843 C ARG 290 52.847 7.567 -1.151 1.00 16.63 ATOM 1844 O ARG 290 53.488 7.832 -2.144 1.00 19.86 ATOM 1845 N LEU 291 51.578 7.914 -1.011 1.00 13.74 ATOM 1846 CA LEU 291 50.849 8.592 -2.084 1.00 15.52 ATOM 1847 CB LEU 291 49.355 8.420 -1.874 1.00 13.32 ATOM 1848 CG LEU 291 48.362 8.707 -2.984 1.00 16.72 ATOM 1849 CD1 LEU 291 48.440 7.651 -4.049 1.00 17.92 ATOM 1850 CD2 LEU 291 47.010 8.654 -2.355 1.00 17.47 ATOM 1851 C LEU 291 51.231 10.077 -2.104 1.00 18.05 ATOM 1852 O LEU 291 51.168 10.722 -3.145 1.00 20.46 ATOM 1853 N TYR 292 51.564 10.638 -0.941 1.00 16.65 ATOM 1854 CA TYR 292 51.995 12.028 -0.857 1.00 15.57 ATOM 1855 CB TYR 292 50.999 12.900 -0.118 1.00 13.30 ATOM 1856 CG TYR 292 49.652 13.041 -0.770 1.00 17.69 ATOM 1857 CD1 TYR 292 48.642 12.118 -0.519 1.00 14.60 ATOM 1858 CE1 TYR 292 47.386 12.269 -1.084 1.00 11.38 ATOM 1859 CD2 TYR 292 49.372 14.125 -1.614 1.00 14.26 ATOM 1860 CE2 TYR 292 48.125 14.279 -2.186 1.00 9.45 ATOM 1861 CZ TYR 292 47.136 13.349 -1.913 1.00 13.74 ATOM 1862 OH TYR 292 45.880 13.498 -2.464 1.00 19.44 ATOM 1863 C TYR 292 53.248 12.005 -0.040 1.00 17.77 ATOM 1864 O TYR 292 53.188 12.265 1.140 1.00 21.18 ATOM 1865 N SER 293 54.388 11.715 -0.652 1.00 17.12 ATOM 1866 CA SER 293 55.630 11.650 0.098 1.00 18.41 ATOM 1867 CB SER 293 56.527 10.586 -0.502 1.00 22.40 ATOM 1868 OG SER 293 57.151 11.100 -1.661 1.00 17.65 ATOM 1869 C SER 293 56.437 12.927 0.177 1.00 20.90 ATOM 1870 O SER 293 57.334 13.013 1.008 1.00 27.08 ATOM 1871 N LYS 294 56.134 13.911 -0.672 1.00 21.04 ATOM 1872 CA LYS 294 56.899 15.174 -0.741 1.00 21.20 ATOM 1873 CB LYS 294 56.888 15.687 -2.188 1.00 24.69 ATOM 1874 CG LYS 294 57.667 14.826 -3.155 1.00 30.89 ATOM 1875 CD LYS 294 57.400 15.182 -4.601 1.00 36.85 ATOM 1876 CE LYS 294 58.381 14.457 -5.546 1.00 40.74 ATOM 1877 NZ LYS 294 58.259 12.949 -5.574 1.00 49.08 ATOM 1878 C LYS 294 56.464 16.329 0.148 1.00 21.21 ATOM 1879 O LYS 294 57.117 17.375 0.194 1.00 24.04 ATOM 1880 N GLY 295 55.374 16.150 0.863 1.00 19.05 ATOM 1881 CA GLY 295 54.852 17.243 1.660 1.00 23.45 ATOM 1882 C GLY 295 53.652 17.716 0.870 1.00 19.08 ATOM 1883 O GLY 295 53.586 17.408 -0.305 1.00 25.31 ATOM 1884 N VAL 296 52 691 18.410 1.466 1.00 16.95 ATOM 1885 CA VAL 296 51.539 18.844 0.690 1.00 17.59 ATOM 1886 CB VAL 296 50.299 17.958 0.980 1.00 15.37 ATOM 1887 CG1 VAL 296 49.139 18.372 0.110 1.00 11.50 ATOM 1888 CG2 VAL 296 50.612 16.502 0.708 1.00 18.57 ATOM 1889 C VAL 296 51.182 20.302 0.956 1.00 20.48 ATOM 1890 O VAL 296 51.102 20.722 2.108 1.00 27.73 ATOM 1891 N LYS 297 50.985 21.077 -0.106 1.00 19.95 ATOM 1892 CA LYS 297 50.604 22.472 0.027 1.00 19.51 ATOM 1893 CB LYS 297 51.444 23.358 -0.888 1.00 21.95 ATOM 1894 CG LYS 297 51.011 24.799 -0.891 1.00 23.34 ATOM 1895 CD LYS 297 51.814 25.617 -1.892 1.00 24.37 ATOM 1896 CE LYS 297 51.247 27.021 -2.068 1.00 24.23 ATOM 1897 NZ LYS 297 49.881 27.038 -2.664 1.00 23.46 ATOM 1898 C LYS 297 49.143 22.532 -0.371 1.00 20.96 ATOM 1899 O LYS 297 48.816 22.330 -1.533 1.00 21.98 ATOM 1900 N THR 298 48.268 22.633 0.626 1.00 21.00 ATOM 1901 CA THR 298 46.839 22.728 0.400 1.00 22.17 ATOM 1902 CB THR 298 46.094 21.394 0.679 1.00 24.36 ATOM 1903 OG1 THR 298 44.705 21.551 0.328 1.00 21.16 ATOM 1904 CG2 THR 298 46.242 20.949 2.132 1.00 13.02 ATOM 1905 C THR 298 46.203 23.850 1.210 1.00 21.58 ATOM 1906 O THR 298 46.881 24.562 1.936 1.00 22.42 ATOM 1907 N GLU 299 44.897 24.020 1.069 1.00 20.01 ATOM 1908 CA GLU 299 44.202 25.069 1.790 1.00 23.19 ATOM 1909 CB GLU 299 44.394 26.388 1.028 1.00 21.52 ATOM 1910 CG GLU 299 44.111 26.241 -0.457 1.00 24.08 ATOM 1911 CD GLU 299 44.281 27.511 -1.246 1.00 21.25 ATOM 1912 OE1 GLU 299 43.347 27.904 -1.952 1.00 23.36 ATOM 1913 OE2 GLU 299 45.363 28.099 -1.199 1.00 25.32 ATOM 1914 C GLU 299 42.709 24.689 1.942 1.00 22.52 ATOM 1915 O GLU 299 42.226 23.799 1.218 1.00 21.89 ATOM 1916 N LEU 300 42.031 25.288 2.935 1.00 18.80 ATOM 1917 CA LEU 300 40.599 25.057 3.208 1.00 17.80 ATOM 1918 CB LEU 300 40.346 24.957 4.716 1.00 18.20 ATOM 1919 CG LEU 300 41.052 23.781 5.409 1.00 18.16 ATOM 1920 CD1 LEU 300 41.281 24.050 6.878 1.00 22.65 ATOM 1921 CD2 LEU 300 40.232 22.548 5.238 1.00 21.52 ATOM 1922 C LEU 300 39.835 26.246 2.626 1.00 15.99 ATOM 1923 O LEU 300 40.070 27.384 3.019 1.00 15.87 ATOM 1924 N THR 301 38.920 25.988 1.697 1.00 16.43 ATOM 1925 CA THR 301 38.198 27.078 1.039 1.00 16.67 ATOM 1926 CB THR 301 38.204 26.860 -0.486 1.00 15.99 ATOM 1927 OG1 THR 301 37.397 25.725 -0.795 1.00 17.35 ATOM 1928 CG2 THR 301 39.629 26.604 -1.001 1.00 12.86 ATOM 1929 C THR 301 36.750 27.381 1.451 1.00 16.97 ATOM 1930 O THR 301 36.115 28.216 0.849 1.00 20.08 ATOM 1931 N ARG 302 36.239 26.775 2.509 1.00 20.61 ATOM 1932 CA ARG 302 34.849 27.007 2.891 1.00 21.32 ATOM 1933 CB ARG 302 34.287 25.864 3.750 1.00 18.48 ATOM 1934 CG ARG 302 34.722 25.893 5.198 1.00 14.88 ATOM 1935 CD ARG 302 36.172 25.671 5.287 1.00 9.35 ATOM 1936 NE ARG 302 36.696 25.844 6.621 1.00 20.42 ATOM 1937 CZ ARG 302 37.108 27.008 7.107 1.00 22.97 ATOM 1938 NH1 ARG 302 37.594 27.070 8.346 1.00 22.13 ATOM 1939 NH2 ARG 302 36.999 28.107 6.368 1.00 17.69 ATOM 1940 C ARG 302 34.591 28.299 3.621 1.00 20.20 ATOM 1941 O ARG 302 35.471 28.855 4.271 1.00 17.57 ATOM 1942 N ASP 303 33.346 28.737 3.495 1.00 25.15 ATOM 1943 CA ASP 303 32.809 29.930 4.140 1.00 26.98 ATOM 1944 CB ASP 303 31.470 30.313 3.515 1.00 26.18 ATOM 1945 CG ASP 303 31.601 30.933 2.177 1.00 29.18 ATOM 1946 OD1 ASP 303 32.703 31.375 1.800 1.00 37.69 ATOM 1947 OD2 ASP 303 30.568 31.017 1.497 1.00 35.54 ATOM 1948 C ASP 303 32.469 29.534 5.571 1.00 28.25 ATOM 1949 O ASP 303 31.989 28.421 5.828 1.00 31.50 ATOM 1950 N ILE 304 32.606 30.486 6.475 1.00 26.71 ATOM 1951 CA ILE 304 32.283 30.267 7.862 1.00 25.31 ATOM 1952 CB ILE 304 33.569 30.156 8.723 1.00 22.72 ATOM 1953 CG2 ILE 304 33.322 30.558 10.144 1.00 20.05 ATOM 1954 CG1 ILE 304 34.034 28.714 8.723 1.00 19.75 ATOM 1955 CD1 ILE 304 32.954 27.806 9.196 1.00 14.92 ATOM 1956 C ILE 304 31.423 31.448 8.250 1.00 26.33 ATOM 1957 O ILE 304 31.748 32.595 7.922 1.00 25.80 ATOM 1958 N PHE 305 30.268 31.152 8.835 1.00 28.50 ATOM 1959 CA PHE 305 29.344 32.188 9.293 1.00 31.16 ATOM 1960 CB PHE 305 27.912 31.852 8.877 1.00 36.40 ATOM 1961 CG PHE 305 27.662 32.026 7.432 1.00 42.07 ATOM 1962 CD1 PHE 305 27.899 30.985 6.549 1.00 46.03 ATOM 1963 CD2 PHE 305 27.261 33.254 6.938 1.00 49.89 ATOM 1964 CE1 PHE 305 27.752 31.156 5.185 1.00 49.49 ATOM 1965 CE2 PHE 305 27.106 33.446 5.571 1.00 54.89 ATOM 1966 CZ PHE 305 27.357 32.389 4.689 1.00 54.32 ATOM 1967 C PHE 305 29.375 32.382 10.814 1.00 29.64 ATOM 1968 O PHE 305 28.992 31.475 11.567 1.00 25.99 ATOM 1969 N THR 306 29.882 33.533 11.261 1.00 28.12 ATOM 1970 CA THR 306 29.873 33.837 12.679 1.00 28.81 ATOM 1971 CB THR 306 30.779 35.048 13.049 1.00 26.16 ATOM 1972 OG1 THR 306 30.624 36.078 12.082 1.00 27.19 ATOM 1973 CG2 THR 306 32.246 34.647 13.127 1.00 20.81 ATOM 1974 C THR 306 28.387 34.136 12.965 1.00 30.50 ATOM 1975 O THR 306 27.599 34.289 12.034 1.00 32.53 ATOM 1976 N ASP 307 27.981 34.164 14.229 1.00 30.85 ATOM 1977 CA ASP 307 26.582 34.411 14.551 1.00 28.56 ATOM 1978 CB ASP 307 26.331 34.154 16.028 1.00 27.80 ATOM 1979 CG ASP 307 26.639 32.741 16.427 1.00 25.34 ATOM 1980 OD1 ASP 307 26.394 31.814 15.621 1.00 27.45 ATOM 1981 OD2 ASP 307 27.126 32.565 17.556 1.00 26.95 ATOM 1982 C ASP 307 26.203 35.830 14.234 1.00 29.47 ATOM 1983 O ASP 307 27.060 36.690 14.098 1.00 32.38 ATOM 1984 N PRO 308 24.905 36.104 14.119 1.00 32.45 ATOM 1985 CD PRO 308 23.768 35.163 14.163 1.00 31.35 ATOM 1986 CA PRO 308 24.467 37.472 13.815 1.00 34.04 ATOM 1987 CB PRO 308 22.958 37.360 13.956 1.00 34.15 ATOM 1988 CG PRO 308 22.694 35.936 13.472 1.00 32.85 ATOM 1989 C PRO 308 25.098 38.483 14.800 1.00 37.93 ATOM 1990 O PRO 308 25.202 38.187 15.998 1.00 37.44 ATOM 1991 N ILE 309 25.503 39.659 14.296 1.00 40.34 ATOM 1992 CA ILE 309 26.182 40.696 15.097 1.00 43.93 ATOM 1993 CB ILE 309 26.369 42.034 14.319 1.00 48.28 ATOM 1994 CG2 ILE 309 26.862 43.148 15.252 1.00 51.65 ATOM 1995 CG1 ILE 309 27.437 41.892 13.240 1.00 49.09 ATOM 1996 CD1 ILE 309 27.842 43.242 12.649 1.00 46.27 ATOM 1997 C ILE 309 25.651 40.995 16.506 1.00 44.62 ATOM 1998 O ILE 309 26.432 41.296 17.431 1.00 41.13 ATOM 1999 N PHE 310 24.341 41.003 16.675 1.00 42.38 ATOM 2000 CA PHE 310 23.843 41.236 18.003 1.00 41.16 ATOM 2001 CB PHE 310 23.491 42.705 18.235 1.00 44.88 ATOM 2002 CG PHE 310 22.411 43.235 17.351 1.00 44.58 ATOM 2003 CD1 PHE 310 21.077 43.166 17.747 1.00 44.20 ATOM 2004 CD2 PHE 310 22.724 43.860 16.159 1.00 38.66 ATOM 2005 CE1 PHE 310 20.076 43.717 16.967 1.00 42.71 ATOM 2006 CE2 PHE 310 21.735 44.406 15.386 1.00 41.33 ATOM 2007 CZ PHE 310 20.404 44.337 15.789 1.00 42.16 ATOM 2008 C PHE 310 22.717 40.301 18.347 1.00 44.75 ATOM 2009 O PHE 310 21.985 39.837 17.482 1.00 43.78 ATOM 2010 N SER 311 22.633 39.981 19.627 1.00 51.28 ATOM 2011 CA SER 311 21.629 39.064 20.151 1.00 56.76 ATOM 2012 CB SER 311 22.166 38.462 21.440 1.00 58.74 ATOM 2013 OG SER 311 23.083 39.374 22.031 1.00 61.15 ATOM 2014 C SER 311 20.271 39.696 20.410 1.00 57.21 ATOM 2015 O SER 311 20.125 40.505 21.328 1.00 59.60 ATOM 2016 N LEU 312 19.275 39.303 19.625 1.00 57.51 ATOM 2017 CA LEU 312 17.921 39.828 19.779 1.00 58.49 ATOM 2018 CB LEU 312 17.065 39.425 18.573 1.00 53.40 ATOM 2019 CG LEU 312 17.575 39.521 17.136 1.00 49.68 ATOM 2020 CD1 LEU 312 16.401 39.249 16.208 1.00 45.27 ATOM 2021 CD2 LEU 312 18.174 40.885 16.843 1.00 49.90 ATOM 2022 C LEU 312 17.316 39.231 21.057 1.00 60.36 ATOM 2023 O LEU 312 16.569 38.269 21.001 1.00 64.66 ATOM 2024 N ASN 313 17.651 39.786 22.210 1.00 60.93 ATOM 2025 CA ASN 313 17.137 39.258 23.471 1.00 63.91 ATOM 2026 CB ASN 313 17.737 40.037 24.667 1.00 71.17 ATOM 2027 CG ASN 313 17.813 41.566 24.434 1.00 75.38 ATOM 2028 OD1 ASN 313 16.997 42.160 23.718 1.00 78.86 ATOM 2029 ND2 ASN 313 18.789 42.199 25.067 1.00 76.26 ATOM 2030 C ASN 313 15.601 39.188 23.555 1.00 62.62 ATOM 2031 O ASN 313 14.989 38.133 23.364 1.00 59.81 ATOM 2032 N THR 314 14.990 40.330 23.839 1.00 61.63 ATOM 2033 CA THR 314 13.549 40.458 23.948 1.00 57.86 ATOM 2034 CB THR 314 13.217 41.790 24.674 1.00 58.51 ATOM 2035 OG1 THR 314 13.881 41.819 25.946 1.00 58.32 ATOM 2036 CG2 THR 314 11.724 41.947 24.888 1.00 59.87 ATOM 2037 C THR 314 12.970 40.457 22.523 1.00 55.92 ATOM 2038 O THR 314 11.767 40.260 22.327 1.00 55.62 ATOM 2039 N LEU 315 13.856 40.624 21.537 1.00 52.11 ATOM 2040 CA LEU 315 13.486 40.683 20.122 1.00 49.01 ATOM 2041 CB LEU 315 14.320 41.757 19.404 1.00 50.14 ATOM 2042 CG LEU 315 14.328 43.217 19.874 1.00 50.23 ATOM 2043 CD1 LEU 315 14.815 44.078 18.718 1.00 51.73 ATOM 2044 CD2 LEU 315 12.933 43.680 20.328 1.00 47.63 ATOM 2045 C LEU 315 13.621 39.375 19.347 1.00 47.16 ATOM 2046 O LEU 315 13.292 39.312 18.157 1.00 43.27 ATOM 2047 N GLN 316 14.097 38.340 20.023 1.00 47.36 ATOM 2048 CA GLN 316 14.311 37.036 19.414 1.00 48.53 ATOM 2049 CB GLN 316 14.411 35.977 20.510 1.00 51.64 ATOM 2050 CG GLN 316 15.051 34.673 20.073 1.00 57.31 ATOM 2051 CD GLN 316 16.565 34.769 19.894 1.00 60.35 ATOM 2052 OE1 GLN 316 17.108 35.810 19.506 1.00 60.96 ATOM 2053 NE2 GLN 316 17.254 33.665 20.169 1.00 63.62 ATOM 2054 C GLN 316 13.200 36.663 18.451 1.00 49.57 ATOM 2055 O GLN 316 13.454 36.241 17.320 1.00 50.18 ATOM 2056 N GLU 317 11.968 36.870 18.901 1.00 48.85 ATOM 2057 CA GLU 317 10.775 36.544 18.126 1.00 52.71 ATOM 2058 CB GLU 317 9.501 36.796 18.953 1.00 60.20 ATOM 2059 CG GLU 317 9.493 36.204 20.377 1.00 70.71 ATOM 2060 CD GLU 317 9.881 37.227 21.456 1.00 76.72 ATOM 2061 OE1 GLU 317 9.273 38.333 21.480 1.00 77.12 ATOM 2062 OE2 GLU 317 10.787 36.920 22.274 1.00 77.99 ATOM 2063 C GLU 317 10.657 37.293 16.799 1.00 48.71 ATOM 2064 O GLU 317 10.071 36.780 15.844 1.00 48.70 ATOM 2065 N TYR 318 11.214 38.494 16.739 1.00 43.49 ATOM 2066 CA TYR 318 11.129 39.300 15.538 1.00 39.92 ATOM 2067 CB TYR 318 10.999 40.761 15.918 1.00 42.45 ATOM 2068 CG TYR 318 9.803 40.971 16.782 1.00 42.68 ATOM 2069 CD1 TYR 318 9.946 41.197 18.144 1.00 40.60 ATOM 2070 CE1 TYR 318 8.849 41.304 18.969 1.00 40.01 ATOM 2071 CD2 TYR 318 8.526 40.860 16.260 1.00 38.85 ATOM 2072 CE2 TYR 318 7.424 40.969 17.078 1.00 40.89 ATOM 2073 CZ TYR 318 7.593 41.189 18.437 1.00 39.14 ATOM 2074 OH TYR 318 6.503 41.297 19.273 1.00 45.54 ATOM 2075 C TYR 318 12.233 39.130 14.522 1.00 37.64 ATOM 2076 O TYR 318 12.303 39.886 13.561 1.00 38.76 ATOM 2077 N GLY 319 13.093 38.141 14.703 1.00 35.33 ATOM 2078 CA GLY 319 14.154 37.962 13.733 1.00 31.25 ATOM 2079 C GLY 319 13.662 37.273 12.476 1.00 30.50 ATOM 2080 O GLY 319 12.575 36.689 12.500 1.00 32.90 ATOM 2081 N PRO 320 14.385 37.395 11.344 1.00 26.91 ATOM 2082 CD PRO 320 15.499 38.333 11.174 1.00 23.64 ATOM 2083 CA PRO 320 14.061 36.776 10.053 1.00 29.07 ATOM 2084 CB PRO 320 15.295 37.106 9.210 1.00 29.08 ATOM 2085 CG PRO 320 16.336 37.590 10.207 1.00 28.14 ATOM 2086 C PRO 320 13.880 35.251 10.152 1.00 30.61 ATOM 2087 O PRO 320 14.650 34.591 10.831 1.00 32.60 ATOM 2088 N THR 321 12.899 34.685 9.451 1.00 32.83 ATOM 2089 CA THR 321 12.676 33.245 9.523 1.00 36.83 ATOM 2090 CB THR 321 11.362 32.782 8.776 1.00 41.13 ATOM 2091 OG1 THR 321 11.482 32.904 7.346 1.00 35.95 ATOM 2092 CG2 THR 321 10.177 33.597 9.267 1.00 40.68 ATOM 2093 C THR 321 13.871 32.438 9.041 1.00 37.20 ATOM 2094 O THR 321 14.789 32.985 8.429 1.00 41.10 ATOM 2095 N PHE 322 13.873 31.149 9.369 1.00 38.20 ATOM 2096 CA PHE 322 14.941 30.216 8.993 1.00 36.64 ATOM 2097 CB PHE 322 14.548 28.794 9.455 1.00 35.09 ATOM 2098 CG PHE 322 15.669 27.776 9.400 1.00 37.60 ATOM 2099 CD1 PHE 322 16.356 27.416 10.554 1.00 36.41 ATOM 2101 CE1 PHE 322 17.359 26.466 10.505 1.00 32.41 ATOM 2102 CE2 PHE 322 17.012 26.216 8.159 1.00 25.56 ATOM 2103 CZ PHE 322 17.682 25.872 9.307 1.00 28.83 ATOM 2104 C PHE 322 15.139 30.260 7.470 1.00 34.25 ATOM 2105 O PHE 322 16.191 30.671 6.987 1.00 26.49 ATOM 2106 N LEU 323 14.081 29.907 6.739 1.00 36.36 ATOM 2107 CA LEU 323 14.078 29.876 5.281 1.00 39.50 ATOM 2108 CB LEU 323 12.713 29.427 4.739 1.00 46.13 ATOM 2109 CG LEU 323 12.323 27.951 4.927 1.00 50.61 ATOM 2110 CD1 LEU 323 10.873 27.714 4.506 1.00 52.63 ATOM 2111 CD2 LEU 323 13.267 27.041 4.131 1.00 52.44 ATOM 2112 C LEU 323 14.486 31.183 4.627 1.00 41.16 ATOM 2113 O LEU 323 15.230 31.174 3.651 1.00 45.33 ATOM 2114 N SER 324 14.006 32.310 5.132 1.00 40.97 ATOM 2115 CA SER 324 14.400 33.583 4.545 1.00 43.00 ATOM 2116 CB SER 324 13.565 34.730 5.111 1.00 47.79 ATOM 2117 OG SER 324 13.504 34.673 6.527 1.00 60.21 ATOM 2118 C SER 324 15.892 33.840 4.774 1.00 40.32 ATOM 2119 O SER 324 16.524 34.581 4.031 1.00 40.93 ATOM 2120 N ILE 325 16.457 33.237 5.808 1.00 38.03 ATOM 2121 CA ILE 325 17.863 33.420 6.060 1.00 35.42 ATOM 2122 CB ILE 325 18.206 33.218 7.502 1.00 32.99 ATOM 2123 CG2 ILE 325 19.698 33.445 7.696 1.00 32.52 ATOM 2124 CG1 ILE 325 17.402 34.213 8.338 1.00 29.14 ATOM 2125 CD1 ILE 325 17.483 33.959 9.785 1.00 28.48 ATOM 2126 C ILE 325 18.647 32.464 5.204 1.00 36.75 ATOM 2127 O ILE 325 19.540 32.893 4.493 1.00 35.77 ATOM 2128 N GLU 326 18.280 31.181 5.228 1.00 41.70 ATOM 2129 CA GLU 326 18.958 30.159 4.420 1.00 45.37 ATOM 2130 CB GLU 326 18.567 28.733 4.849 1.00 44.39 ATOM 2131 CG GLU 326 19.363 28.140 6.032 1.00 46.63 ATOM 2132 CD GLU 326 20.865 27.938 5.771 1.00 48.09 ATOM 2133 OE1 GLU 326 21.672 28.753 6.258 1.00 47.88 ATOM 2134 OE2 GLU 326 21.253 26.941 5.126 1.00 50.34 ATOM 2135 C GLU 326 18.733 30.312 2.908 1.00 47.91 ATOM 2136 O GLU 326 19.515 29.795 2.113 1.00 52.83 ATOM 2137 N ASN 327 17.667 30.992 2.503 1.00 49.53 ATOM 2138 CA ASN 327 17.392 31.186 1.077 1.00 50.26 ATOM 2139 CB ASN 327 15.883 31.067 0.785 1.00 57.24 ATOM 2140 CG ASN 327 15.348 29.639 0.923 1.00 63.35 ATOM 2141 OD1 ASN 327 14.362 29.271 0.272 1.00 65.72 ATOM 2142 ND2 ASN 327 15.973 28.838 1.787 1.00 66.61 ATOM 2143 C ASN 327 17.885 32.557 0.602 1.00 49.12 ATOM 2144 O ASN 327 17.732 32.910 -0.566 1.00 48.41 ATOM 2145 N SER 328 18.460 33.336 1.513 1.00 48.24 ATOM 2146 CA SER 328 18.940 34.666 1.177 1.00 44.37 ATOM 2147 CB SER 328 18.354 35.682 2.141 1.00 43.90 ATOM 2148 OG SER 328 18.337 36.973 1.573 1.00 53.23 ATOM 2149 C SER 328 20.448 34.713 1.234 1.00 42.82 ATOM 2150 O SER 328 21.068 35.599 0.662 1.00 44.52 ATOM 2151 N ILE 329 21.043 33.789 1.973 1.00 41.88 ATOM 2152 CA ILE 329 22.489 33.739 2.053 1.00 43.60 ATOM 2153 CB ILE 329 23.002 32.593 2.976 1.00 47.00 ATOM 2154 CG2 ILE 329 24.519 32.637 3.053 1.00 51.01 ATOM 2155 CG1 ILE 329 22.439 32.700 4.395 1.00 45.80 ATOM 2156 CD1 ILE 329 23.249 33.560 5.348 1.00 51.95 ATOM 2157 C ILE 329 22.993 33.464 0.632 1.00 44.62 ATOM 2158 O ILE 329 22.281 32.911 -0.215 1.00 42.08 ATOM 2159 N ARG 330 24.244 33.838 0.409 1.00 47.30 ATOM 2160 CA ARG 330 24.963 33.693 -0.851 1.00 46.81 ATOM 2161 CB ARG 330 26.279 34.416 -0.638 1.00 45.98 ATOM 2162 CG ARG 330 27.046 34.848 -1.827 1.00 44.32 ATOM 2163 CD ARG 330 28.355 35.373 -1.277 1.00 42.48 ATOM 2164 NE ARG 330 29.270 35.765 -2.322 1.00 38.20 ATOM 2165 CZ ARG 330 30.584 35.790 -2.188 1.00 34.54 ATOM 2166 NH1 ARG 330 31.303 36.170 -3.213 1.00 39.28 ATOM 2167 NH2 ARG 330 31.172 35.436 -1.056 1.00 32.79 ATOM 2168 C ARG 330 25.214 32.203 -1.154 1.00 47.48 ATOM 2169 O ARG 330 25.815 31.492 -0.345 1.00 49.75 ATOM 2170 N LYS 331 24.788 31.735 -2.323 1.00 44.85 ATOM 2171 CA LYS 331 24.965 30.321 -2.677 1.00 45.45 ATOM 2172 CB LYS 331 23.947 29.905 -3.755 1.00 47.94 ATOM 2173 CG LYS 331 23.989 30.723 -5.023 1.00 58.90 ATOM 2174 CD LYS 331 22.834 30.357 -5.938 1.00 66.64 ATOM 2175 CE LYS 331 22.853 31.194 -7.215 1.00 71.89 ATOM 2176 NZ LYS 331 21.564 31.088 -7.969 1.00 75.69 ATOM 2177 C LYS 331 26.413 29.994 -3.086 1.00 39.16 ATOM 2178 O LYS 331 27.229 30.912 -3.208 1.00 35.42 ATOM 2179 N PRO 332 26.759 28.687 -3.243 1.00 36.88 ATOM 2180 CD PRO 332 25.907 27.510 -2.988 1.00 34.11 ATOM 2181 CA PRO 332 28.113 28.249 -3.627 1.00 35.07 ATOM 2182 CB PRO 332 27.952 26.732 -3.834 1.00 31.43 ATOM 2183 CG PRO 332 26.465 26.521 -3.945 1.00 34.71 ATOM 2184 C PRO 332 28.695 28.993 -4.837 1.00 33.27 ATOM 2185 O PRO 332 28.069 29.092 -5.891 1.00 32.47 ATOM 2186 N HIS 333 29.927 29.464 -4.675 1.00 31.69 ATOM 2187 CA HIS 333 30.592 30.283 -5.677 1.00 29.36 ATOM 2188 CB HIS 333 30.345 31.755 -5.284 1.00 29.61 ATOM 2189 CG HIS 333 30.759 32.078 -3.874 1.00 31.85 ATOM 2190 CD2 HIS 333 31.978 32.349 -3.343 1.00 30.11 ATOM 2191 ND1 HIS 333 29.879 32.052 -2.811 1.00 32.89 ATOM 2192 CE1 HIS 333 30.540 32.282 -1.688 1.00 33.67 ATOM 2193 NE2 HIS 333 31.815 32.467 -1.984 1.00 27.12 ATOM 2194 C HIS 333 32.106 30.062 -5.781 1.00 25.03 ATOM 2195 O HIS 333 32.719 29.414 -4.936 1.00 25.48 ATOM 2196 N LEU 334 32.706 30.630 -6.817 1.00 23.62 ATOM 2197 CA LEU 334 34.156 30.561 -6.982 1.00 25.27 ATOM 2198 CB LEU 334 34.615 31.210 -8.298 1.00 20.89 ATOM 2199 CG LEU 334 34.198 30.552 -9.612 1.00 21.30 ATOM 2200 CD1 LEU 334 34.810 31.273 -10.809 1.00 16.30 ATOM 2201 CD2 LEU 334 34.625 29.094 -9.573 1.00 19.51 ATOM 2202 C LEU 334 34.668 31.415 -5.837 1.00 25.83 ATOM 2203 O LEU 334 34.023 32.389 -5.461 1.00 27.82 ATOM 2204 N PHE 335 35.832 31.077 -5.306 1.00 27.75 ATOM 2205 CA PHE 335 36.413 31.821 -4.195 1.00 24.44 ATOM 2206 CB PHE 335 37.718 31.140 -3.764 1.00 25.26 ATOM 2207 CG PHE 335 38.196 31.546 -2.403 1.00 27.14 ATOM 2208 CD1 PHE 335 37.761 30.866 -1.269 1.00 27.42 ATOM 2209 CD2 PHE 335 39.077 32.609 -2.249 1.00 29.95 ATOM 2210 CE1 PHE 335 38.191 31.246 -0.002 1.00 31.73 ATOM 2211 CE2 PHE 335 39.514 32.997 -0.983 1.00 31.29 ATOM 2212 CZ PHE 335 39.073 32.318 0.141 1.00 29.70 ATOM 2213 C PHE 335 36.719 33.250 -4.601 1.00 21.92 ATOM 2214 O PHE 335 37.287 33.463 -5.653 1.00 23.54 ATOM 2215 N ASP 336 36.340 34.217 -3.772 1.00 21.21 ATOM 2216 CA ASP 336 36.652 35.623 -4.018 1.00 21.48 ATOM 2217 CB ASP 336 35.525 36.386 -4.718 1.00 23.79 ATOM 2218 CG ASP 336 34.172 36.174 -4.083 1.00 23.35 ATOM 2219 OD1 ASP 336 34.038 36.239 -2.844 1.00 22.38 ATOM 2220 OD2 ASP 336 33.228 35.955 -4.868 1.00 31.58 ATOM 2221 C ASP 336 37.061 36.300 -2.715 1.00 22.29 ATOM 2222 O ASP 336 36.904 35.720 -1.661 1.00 25.71 ATOM 2223 N TYR 337 37.518 37.544 -2.788 1.00 20.76 ATOM 2224 CA TYR 337 38.037 38.268 -1.632 1.00 21.98 ATOM 2225 CB TYR 337 39.538 38.538 -1.877 1.00 17.10 ATOM 2226 CG TYR 337 40.339 37.311 -2.313 1.00 17.63 ATOM 2227 CD1 TYR 337 40.203 36.764 -3.590 1.00 20.68 ATOM 2228 CE1 TYR 337 40.875 35.572 -3.955 1.00 23.11 ATOM 2229 CD2 TYR 337 41.178 36.648 -1.415 1.00 23.13 ATOM 2230 CE2 TYR 337 41.854 35.466 -1.766 1.00 23.39 ATOM 2231 CZ TYR 337 41.694 34.934 -3.030 1.00 24.50 ATOM 2232 OH TYR 337 42.330 33.758 -3.332 1.00 26.47 ATOM 2233 C TYR 337 37.305 39.586 -1.400 1.00 22.36 ATOM 2234 O TYR 337 36.807 40.175 -2.333 1.00 24.56 ATOM 2235 N LEU 338 37.283 40.079 -0.170 1.00 26.34 ATOM 2236 CA LEU 338 36.590 41.342 0.121 1.00 29.06 ATOM 2237 CB LEU 338 36.422 41.557 1.642 1.00 28.21 ATOM 2238 CG LEU 338 35.501 42.690 2.150 1.00 25.11 ATOM 2239 CD1 LEU 338 34.056 42.386 1.828 1.00 24.92 ATOM 2240 CD2 LEU 338 35.645 42.872 3.652 1.00 24.77 ATOM 2241 C LEU 338 37.318 42.542 -0.480 1.00 29.54 ATOM 2242 O LEU 338 38.543 42.674 -0.332 1.00 32.83 ATOM 2243 N GLN 339 36.562 43.389 -1.178 1.00 28.15 ATOM 2244 CA GLN 339 37.101 44.605 -1.793 1.00 31.21 ATOM 2245 CB GLN 339 36.617 44.766 -3.242 1.00 40.03 ATOM 2246 CG GLN 339 37.561 44.246 -4.307 1.00 49.91 ATOM 2247 CD GLN 339 38.935 44.882 -4.220 1.00 55.33 ATOM 2248 OE1 GLN 339 39.718 44.570 -3.316 1.00 58.04 ATOM 2249 NE2 GLN 339 39.235 45.786 -5.155 1.00 57.36 ATOM 2250 C GLN 339 36.640 45.818 -1.007 1.00 27.69 ATOM 2251 O GLN 339 37.430 46.720 -0.715 1.00 26.69 ATOM 2252 N GLY 340 35.340 45.869 -0.744 1.00 21.87 ATOM 2253 CA GLY 340 34.800 46.972 0.008 1.00 23.38 ATOM 2254 C GLY 340 33.382 46.720 0.460 1.00 24.89 ATOM 2255 O GLY 340 32.747 45.762 -0.010 1.00 19.77 ATOM 2256 N ILE 341 32.918 47.555 1.400 1.00 27.43 ATOM 2257 CA ILE 341 31.557 47.502 1.942 1.00 27.30 ATOM 2258 CB ILE 341 31.492 47.019 3.422 1.00 27.82 ATOM 2259 CG2 ILE 341 30.028 46.858 3.859 1.00 26.82 ATOM 2260 CG1 ILE 341 32.208 45.678 3.611 1.00 28.32 ATOM 2261 CD1 ILE 341 32.064 45.102 5.021 1.00 20.98 ATOM 2262 C ILE 341 30.975 48.918 1.915 1.00 29.75 ATOM 2263 O ILE 341 31.653 49.893 2.265 1.00 30.81 ATOM 2264 N GLU 342 29.727 49.011 1.471 1.00 29.58 ATOM 2265 CA GLU 342 29.002 50.263 1.393 1.00 29.98 ATOM 2266 CB GLU 342 28.396 50.451 0.001 1.00 33.94 ATOM 2267 CG GLU 342 27.313 51.535 -0.052 1.00 44.76 ATOM 2268 CD GLU 342 26.970 52.004 -1.457 1.00 47.49 ATOM 2269 OE1 GLU 342 27.893 52.466 -2.164 1.00 50.86 ATOM 2270 OE2 GLU 342 25.780 51.935 -1.841 1.00 48.19 ATOM 2271 C GLU 342 27.896 50.242 2.441 1.00 30.01 ATOM 2272 O GLU 342 26.846 49.619 2.267 1.00 30.06 ATOM 2273 N PHE 343 28.135 50.965 3.515 1.00 29.93 ATOM 2274 CA PHE 343 27.213 51.059 4.624 1.00 29.27 ATOM 2275 CB PHE 343 27.986 51.523 5.836 1.00 29.40 ATOM 2276 CG PHE 343 29.021 50.555 6.278 1.00 35.00 ATOM 2277 CD1 PHE 343 30.344 50.708 5.888 1.00 34.33 ATOM 2278 CD2 PHE 343 28.668 49.471 7.087 1.00 34.94 ATOM 2279 CE1 PHE 343 31.301 49.795 6.297 1.00 32.19 ATOM 2280 CE2 PHE 343 29.619 48.555 7.501 1.00 33.61 ATOM 2281 CZ PHE 343 30.940 48.720 7.104 1.00 34.76 ATOM 2282 C PHE 343 26.050 51.998 4.414 1.00 30.11 ATOM 2283 O PHE 343 26.243 53.182 4.128 1.00 31.52 ATOM 2284 N HIS 344 24.841 51.475 4.580 1.00 30.38 ATOM 2285 CA HIS 344 23.624 52.280 4.450 1.00 32.05 ATOM 2286 CB HIS 344 22.596 51.571 3.553 1.00 32.38 ATOM 2287 CG HIS 344 22.806 51.818 2.083 1.00 33.83 ATOM 2288 CD2 HIS 344 23.922 51.755 1.317 1.00 32.02 ATOM 2289 ND1 HIS 344 21.788 52.209 1.238 1.00 30.81 ATOM 2290 CE1 HIS 344 22.265 52.376 0.020 1.00 29.92 ATOM 2291 NE2 HIS 344 23.558 52.106 0.040 1.00 32.00 ATOM 2292 C HIS 344 23.076 52.567 5.855 1.00 30.97 ATOM 2293 O HIS 344 22.927 51.648 6.648 1.00 31.67 ATOM 2294 N THR 345 22.753 53.830 6.142 1.00 31.95 ATOM 2295 CA THR 345 22.290 54.248 7.471 1.00 31.87 ATOM 2296 CB THR 345 23.297 55.247 8.060 1.00 30.01 ATOM 2297 OG1 THR 345 24.621 54.713 7.937 1.00 37.38 ATOM 2298 CG2 THR 345 23.012 55.496 9.513 1.00 34.79 ATOM 2299 C THR 345 20.900 54.861 7.656 1.00 30.45 ATOM 2306 O THR 345 20.481 55.707 6.907 1.00 30.35 ATOM 2301 N ARG 346 20.239 54.514 8.742 1.00 29.47 ATOM 2302 CA ARG 346 18.931 55.064 9.021 1.00 33.75 ATOM 2303 CB ARG 346 17.846 54.082 8.623 1.00 31.11 ATOM 2304 CG ARG 346 17.570 54.113 7.156 1.00 37.30 ATOM 2305 CD ARG 346 16.698 52.963 6.778 1.00 40.39 ATOM 2306 NE ARG 346 15.435 53.390 6.214 1.00 45.12 ATOM 2307 CZ ARG 346 14.267 53.208 6.816 1.00 53.06 ATOM 2308 NH1 ARG 346 13.159 53.615 6.225 1.00 59.78 ATOM 2309 NH2 ARG 346 14.197 52.647 8.015 1.00 55.83 ATOM 2310 C ARG 346 18.791 55.423 10.490 1.00 35.43 ATOM 2311 O ARG 346 19.589 54.982 11.323 1.00 36.81 ATOM 2312 N LEU 347 17.823 56.288 10.788 1.00 37.54 ATOM 2313 CA LEU 347 17.548 56.712 12.156 1.00 36.68 ATOM 2314 CB LEU 347 17.019 58.138 12.180 1.00 38.30 ATOM 2315 CG LEU 347 16.484 58.548 13.554 1.00 41.60 ATOM 2316 CD1 LEU 347 17.617 58.883 14.514 1.00 42.74 ATOM 2317 CD2 LEU 347 15.558 59.708 13.397 1.00 42.70 ATOM 2318 C LEU 347 16.515 55.776 12.800 1.00 37.67 ATOM 2319 O LEU 347 15.596 55.282 12.136 1.00 39.32 ATOM 2320 N GLN 348 16.699 55.528 14.090 1.00 35.33 ATOM 2321 CA GLN 348 15.829 54.669 14.881 1.00 32.60 ATOM 2322 CB GLN 348 16.666 53.583 15.546 1.00 33.20 ATOM 2323 CG GLN 348 15.908 52.659 16.428 1.00 36.04 ATOM 2324 CD GLN 348 14.852 51.898 15.687 1.00 41.50 ATOM 2325 OE1 GLN 348 13.702 52.330 15.616 1.00 40.24 ATOM 2326 NE2 GLN 348 15.219 50.731 15.162 1.00 43.99 ATOM 2327 C GLN 348 15.321 55.653 15.905 1.00 31.09 ATOM 2328 O GLN 348 16.075 56.120 16.753 1.00 32.14 ATOM 2329 N PRO 349 14.058 56.060 15.784 1.00 31.17 ATOM 2330 CD PRO 349 13.063 55.775 14.740 1.00 32.17 ATOM 2331 CA PRO 349 13.533 57.021 16.739 1.00 33.71 ATOM 2332 CB PRO 349 12.323 57.590 15.993 1.00 33.92 ATOM 2333 CG PRO 349 11.799 56.401 15.298 1.00 29.74 ATOM 2334 C PRO 349 13.140 56.460 18.082 1.00 35.91 ATOM 2335 O PRO 349 12.549 55.381 18.177 1.00 39.64 ATOM 2336 N GLY 350 13.527 57.183 19.124 1.00 34.78 ATOM 2337 CA GLY 350 13.145 56.802 20.463 1.00 29.91 ATOM 2338 C GLY 350 11.810 57.502 20.645 1.00 28.68 ATOM 2339 O GLY 350 11.538 58.539 20.041 1.00 28.73 ATOM 2340 N TYR 351 10.968 56.949 21.492 1.00 31.04 ATOM 2341 CA TYR 351 9.659 57.522 21.748 1.00 28.15 ATOM 2342 CB TYR 351 8.939 56.667 22.782 1.00 25.11 ATOM 2343 CG TYR 351 7.527 57.070 23.026 1.00 28.78 ATOM 2344 CD1 TYR 351 6.530 56.806 22.090 1.00 29.11 ATOM 2345 CE1 TYR 351 5.210 57.197 22.325 1.00 36.47 ATOM 2346 CD2 TYR 351 7.181 57.727 24.199 1.00 32.05 ATOM 2347 CE2 TYR 351 5.879 58.125 24.451 1.00 37.99 ATOM 2348 CZ TYR 351 4.892 57.866 23.517 1.00 40.84 ATOM 2349 OH TYR 351 3.609 58.316 23.786 1.00 43.75 ATOM 2350 C TYR 351 9.751 58.974 22.194 1.00 26.00 ATOM 2351 O TYR 351 8.934 59.786 21.809 1.00 29.53 ATOM 2352 N PHE 352 10.785 59.307 22.952 1.00 28.14 ATOM 2353 CA PHE 352 10.978 60.669 23.442 1.00 30.63 ATOM 2354 CB PHE 352 11.465 60.650 24.891 1.00 34.55 ATOM 2355 CG PHE 352 10.616 59.802 25.810 1.00 40.51 ATOM 2356 CD1 PHE 352 10.934 58.454 26.027 1.00 39.36 ATOM 2357 CD2 PHE 352 9.512 60.356 26.476 1.00 39.04 ATOM 2358 CE1 PHE 352 10.174 57.670 26.891 1.00 40.28 ATOM 2359 CE2 PHE 352 8.743 59.589 27.341 1.00 40.04 ATOM 2360 CZ PHE 352 9.073 58.241 27.551 1.00 43.17 ATOM 2361 C PHE 352 11.942 61.513 22.613 1.00 35.71 ATOM 2362 O PHE 352 12.403 62.556 23.083 1.00 39.58 ATOM 2363 N GLY 353 12.317 61.033 21.426 1.00 36.10 ATOM 2364 CA GLY 353 13.201 61.791 20.549 1.00 37.76 ATOM 2365 C GLY 353 14.656 62.037 20.933 1.00 40.10 ATOM 2366 O GLY 353 15.544 62.011 20.072 1.00 41.93 ATOM 2367 N LYS 354 14.928 62.314 22.196 1.00 37.55 ATOM 2368 CA LYS 354 16.308 62.558 22.585 1.00 40.81 ATOM 2369 CB LYS 354 16.381 63.243 23.966 1.00 46.62 ATOM 2370 CG LYS 354 17.574 64.209 24.106 1.00 50.82 ATOM 2371 CD LYS 354 17.955 64.543 25.558 1.00 55.27 ATOM 2372 CE LYS 354 19.409 65.106 25.624 1.00 59.06 ATOM 2373 NZ LYS 354 19.989 65.226 27.011 1.00 61.08 ATOM 2374 C LYS 354 17.097 61.243 22.597 1.00 39.24 ATOM 2375 O LYS 354 18.321 61.243 22.467 1.00 39.45 ATOM 2376 N ASP 355 16.387 60.130 22.746 1.00 36.63 ATOM 2377 CA ASP 355 17.014 58.811 22.784 1.00 36.64 ATOM 2378 CB ASP 355 16.433 57.956 23.918 1.00 38.81 ATOM 2379 CG ASP 355 14.899 57.893 23.905 1.00 39.86 ATOM 2380 OD1 ASP 355 14.329 57.075 24.666 1.00 39.20 ATOM 2381 OD2 ASP 355 14.258 58.674 23.174 1.00 41.91 ATOM 2382 C ASP 355 16.921 58.048 21.467 1.00 36.41 ATOM 2383 O ASP 355 16.687 56.839 21.459 1.00 39.46 ATOM 2384 N SER 356 17.033 58.767 20.358 1.00 32.11 ATOM 2385 CA SER 356 16.985 58.155 19.049 1.00 31.06 ATOM 2386 CB SER 356 16.313 59.112 18.075 1.00 32.06 ATOM 2387 OG SER 356 15.076 59.546 18.599 1.00 35.15 ATOM 2388 C SER 356 18.426 57.884 18.613 1.00 32.46 ATOM 2389 O SER 356 19.356 58.546 19.091 1.00 33.43 ATOM 2390 N PHE 357 18.635 56.914 17.730 1.00 31.20 ATOM 2391 CA PHE 357 19.994 56.635 17.280 1.00 30.41 ATOM 2392 CB PHE 357 20.662 55.552 18.150 1.00 26.65 ATOM 2393 CG PHE 357 20.023 54.184 18.032 1.00 26.35 ATOM 2394 CD1 PHE 357 20.538 53.228 17.146 1.00 24.89 ATOM 2395 CD2 PHE 357 18.915 53.852 18.797 1.00 25.64 ATOM 2396 CE1 PHE 357 19.963 51.973 17.024 1.00 20.16 ATOM 2397 CE2 PHE 357 18.323 52.588 18.685 1.00 23.45 ATOM 2398 CZ PHE 357 18.851 51.649 17.794 1.00 25.99 ATOM 2399 C PHE 357 20.008 56.223 15.825 1.00 30.71 ATOM 2400 O PHE 357 18.985 55.809 15.275 1.00 29.78 ATOM 2401 N ASN 358 21.155 56.405 15.187 1.00 32.57 ATOM 2402 CA ASN 358 21.326 56.021 13.795 1.00 33.87 ATOM 2403 CB ASN 358 22.252 57.010 13.070 1.00 35.37 ATOM 2404 CG ASN 358 21.633 58.398 12.892 1.00 37.55 ATOM 2405 OD1 ASN 358 22.327 59.358 12.511 1.00 38.07 ATOM 2406 ND2 ASN 358 20.336 58.517 13.162 1.00 37.72 ATOM 2407 C ASN 358 21.954 54.622 13.846 1.00 33.48 ATOM 2408 O ASN 358 22.761 54.341 14.736 1.00 31.82 ATOM 2409 N TYR 359 21.570 53.744 12.924 1.00 33.09 ATOM 2410 CA TYR 359 22.093 52.381 12.901 1.00 33.75 ATOM 2411 CB TYR 359 21.098 51.434 13.563 1.00 33.52 ATOM 2412 CG TYR 359 19.782 51.352 12.818 1.00 34.92 ATOM 2413 CD1 TYR 359 19.449 50.224 12.055 1.00 33.07 ATOM 2414 CE1 TYR 359 18.265 50.165 11.326 1.00 29.76 ATOM 2415 CD2 TYR 359 18.889 52.420 12.834 1.00 37.77 ATOM 2416 CE2 TYR 359 17.696 52.374 12.104 1.00 38.88 ATOM 2417 CZ TYR 359 17.396 51.246 11.354 1.00 36.77 ATOM 2418 OH TYR 359 16.235 51.223 10.618 1.00 35.92 ATOM 2419 C TYR 359 22.231 51.978 11.454 1.00 35.05 ATOM 2420 O TYR 359 21.526 52.545 10.615 1.00 36.86 ATOM 2421 N TRP 360 23.110 51.022 11.128 1.00 34.37 ATOM 2422 CA TRP 360 23.178 50.647 9.731 1.00 32.80 ATOM 2423 CB TRP 360 24.568 50.271 9.210 1.00 38.80 ATOM 2424 CG TRP 360 25.172 48.996 9.571 1.00 40.63 ATOM 2425 CD2 TRP 360 25.669 48.006 8.655 1.00 39.06 ATOM 2426 CE2 TRP 360 26.392 47.049 9.423 1.00 40.29 ATOM 2427 CE3 TRP 360 25.591 47.840 7.275 1.00 27.60 ATOM 2428 CD1 TRP 360 25.564 48.606 10.808 1.00 46.32 ATOM 2429 NE1 TRP 360 26.307 47.437 10.732 1.00 48.10 ATOM 2430 CZ2 TRP 360 27.033 45.945 8.852 1.00 36.63 ATOM 2431 CZ3 TRP 360 26.224 46.743 6.708 1.00 33.68 ATOM 2432 CH2 TRP 360 26.942 45.810 7.498 1.00 36.39 ATOM 2433 C TRP 360 22.091 49.678 9.390 1.00 29.48 ATOM 2434 O TRP 360 21.916 48.662 10.043 1.00 28.40 ATOM 2435 N SER 361 21.291 50.100 8.422 1.00 24.82 ATOM 2436 CA SER 361 20.118 49.390 7.966 1.00 25.01 ATOM 2437 CB SER 361 19.040 50.417 7.657 1.00 25.02 ATOM 2438 OG SER 361 19.534 51.372 6.728 1.00 28.01 ATOM 2439 C SER 361 20.272 48.481 6.770 1.00 25.86 ATOM 2440 O SER 361 19.452 47.584 6.563 1.00 28.24 ATOM 2441 N GLY 362 21.287 48.721 5.955 1.00 26.61 ATOM 2442 CA GLY 362 21.470 47.893 4.775 1.00 26.68 ATOM 2443 C GLY 362 22.843 48.075 4.174 1.00 24.88 ATOM 2444 O GLY 362 23.624 48.876 4.681 1.00 25.16 ATOM 2445 N ASN 363 23.135 47.385 3.078 1.00 24.77 ATOM 2446 CA ASN 363 24.459 47.503 2.494 1.00 25.21 ATOM 2447 CB ASN 363 25.510 46.904 3.453 1.00 21.78 ATOM 2448 CG ASN 363 25.509 45.366 3.479 1.00 24.03 ATOM 2449 OD1 ASN 363 26.521 44.736 3.172 1.00 24.61 ATOM 2450 ND2 ASN 363 24.396 44.762 3.893 1.00 26.86 ATOM 2451 C ASN 363 24.598 46.810 1.166 1.00 28.38 ATOM 2452 O ASN 363 23.737 46.009 0.783 1.00 27.10 ATOM 2453 N TYR 364 25.684 47.158 0.477 1.00 29.28 ATOM 2454 CA TYR 364 26.101 46.545 -0.782 1.00 30.49 ATOM 2455 CB TYR 364 26.241 47.570 -1.888 1.00 30.92 ATOM 2456 CG TYR 364 24.976 47.958 -2.584 1.00 35.24 ATOM 2457 CD1 TYR 364 24.508 49.266 -2.504 1.00 37.00 ATOM 2458 CE1 TYR 364 23.391 49.671 -3.198 1.00 37.99 ATOM 2459 CD2 TYR 364 24.280 47.047 -3.380 1.00 33.35 ATOM 2460 CE2 TYR 364 23.152 47.443 -4.082 1.00 38.54 ATOM 2461 CZ TYR 364 22.717 48.766 -3.983 1.00 38.50 ATOM 2462 OH TYR 364 21.612 49.214 -4.665 1.00 45.95 ATOM 2463 C TYR 364 27.522 46.055 -0.488 1.00 32.98 ATOM 2464 O TYR 364 28.281 46.720 0.230 1.00 33.48 ATOM 2465 N VAL 365 27.899 44.898 -1.005 1.00 34.46 ATOM 2466 CA VAL 365 29.266 44.442 -0.779 1.00 35.26 ATOM 2467 CB VAL 365 29.324 43.174 0.132 1.00 35.22 ATOM 2468 CG1 VAL 365 28.544 42.064 -0.479 1.00 36.06 ATOM 2469 CG2 VAL 365 30.774 42.761 0.415 1.00 32.31 ATOM 2470 C VAL 365 29.946 44.221 -2.124 1.00 32.82 ATOM 2471 O VAL 365 29.287 43.928 -3.127 1.00 29.89 ATOM 2472 N GLU 366 31.239 44.490 -2.164 1.00 30.38 ATOM 2473 CA GLU 366 32.002 44.298 -3.378 1.00 34.07 ATOM 2474 CB GLU 366 32.648 45.606 -3.814 1.00 37.91 ATOM 2475 CG GLU 366 31.688 46.701 -4.249 1.00 41.21 ATOM 2476 CD GLU 366 32.428 47.937 -4.782 1.00 43.61 ATOM 2477 OE1 GLU 366 31.836 48.651 -5.635 1.00 40.82 ATOM 2478 OE2 GLU 366 33.591 48.184 -4.350 1.00 37.47 ATOM 2479 C GLU 366 33.104 43.272 -3.155 1.00 33.05 ATOM 2480 O GLU 366 33.875 43.392 -2.194 1.00 31.68 ATOM 2481 N THR 367 33.169 42.261 -4.021 1.00 32.11 ATOM 2482 CA THR 367 34.217 41.249 -3.923 1.00 31.20 ATOM 2483 CB THR 367 33.687 39.839 -3.496 1.00 27.61 ATOM 2484 OG1 THR 367 32.743 39.357 -4.444 1.00 28.79 ATOM 2485 CG2 THR 367 33.031 39.876 -2.120 1.00 28.94 ATOM 2486 C THR 367 34.979 41.142 -5.241 1.00 29.56 ATOM 2487 O THR 367 34.447 41.405 -6.310 1.00 29.90 ATOM 2488 N ARG 368 36.237 40.756 -5.142 1.00 31.09 ATOM 2489 CA ARG 368 37.123 40.604 -6.284 1.00 31.96 ATOM 2490 CB ARG 368 38.379 41.435 -6.014 1.00 29.37 ATOM 2491 CG ARG 368 39.507 41.187 -6.926 1.00 34.48 ATOM 2492 CD ARG 368 40.493 40.266 -6.273 1.00 41.51 ATOM 2493 NE ARG 368 41.404 39.670 -7.251 1.00 47.48 ATOM 2494 CZ ARG 368 42.269 40.372 -7.971 1.00 51.99 ATOM 2495 NH1 ARG 368 43.070 39.756 -8.839 1.00 54.18 ATOM 2496 NH2 ARG 368 42.336 41.697 -7.820 1.00 53.93 ATOM 2497 C ARG 368 37.451 39.109 -6.444 1.00 33.34 ATOM 2498 O ARG 368 37.763 38.436 -5.464 1.00 34.00 ATOM 2499 N PRO 369 37.391 38.580 -7.680 1.00 34.18 ATOM 2500 CD PRO 369 37.115 39.364 -8.888 1.00 33.71 ATOM 2501 CA PRO 369 37.656 37.186 -8.054 1.00 30.61 ATOM 2502 CB PRO 369 37.481 37.200 -9.561 1.00 31.74 ATOM 2503 CG PRO 369 36.530 38.326 -9.771 1.00 35.33 ATOM 2504 C PRO 369 39.044 36.722 -7.722 1.00 29.83 ATOM 2505 O PRO 369 39.924 37.525 -7.398 1.00 27.32 ATOM 2506 N SER 370 39.255 35.417 -7.836 1.00 28.62 ATOM 2507 CA SER 370 40.573 34.883 -7.554 1.00 31.48 ATOM 2508 CB SER 370 40.546 33.372 -7.433 1.00 27.56 ATOM 2509 OG SER 370 41.406 33.022 -6.370 1.00 38.88 ATOM 2510 C SER 370 41.553 35.358 -8.632 1.00 29.79 ATOM 2511 O SER 370 41.136 35.864 -9.680 1.00 28.74 ATOM 2512 N ILE 371 42.849 35.217 -8.367 1.00 29.17 ATOM 2513 CA ILE 371 43.867 35.686 -9.297 1.00 28.44 ATOM 2514 CB ILE 371 45.288 35.247 -8.863 1.00 24.69 ATOM 2515 CG2 ILE 371 45.532 33.810 -9.203 1.00 24.58 ATOM 2516 CG1 ILE 371 46.322 36.103 -9.586 1.00 29.48 ATOM 2517 CD1 ILE 371 47.658 36.218 -8.891 1.00 30.22 ATOM 2518 C ILE 371 43.560 35.358 -10.778 1.00 28.82 ATOM 2519 O ILE 371 43.096 34.268 -11.119 1.00 28.35 ATOM 2520 N GLY 372 43.745 36.354 -11.637 1.00 30.09 ATOM 2521 CA GLY 372 43.456 36.181 -13.049 1.00 34.56 ATOM 2522 C GLY 372 42.236 36.980 -13.483 1.00 36.19 ATOM 2523 O GLY 372 41.849 36.930 -14.640 1.00 38.57 ATOM 2524 N SER 373 41.608 37.689 -12.549 1.00 40.47 ATOM 2525 CA SER 373 40.446 38.522 -12.841 1.00 41.94 ATOM 2526 CB SER 373 39.187 37.678 -12.980 1.00 41.45 ATOM 2527 OG SER 373 38.126 38.476 -13.463 1.00 43.54 ATOM 2528 C SER 373 40.251 39.574 -11.752 1.00 45.16 ATOM 2529 O SER 373 40.044 39.266 -10.570 1.00 46.16 ATOM 2530 N SER 374 40.308 40.828 -12.157 1.00 48.44 ATOM 2531 CA SER 374 40.162 41.911 -11.202 1.00 53.89 ATOM 2532 CB SER 374 41.048 43.071 -11.625 1.00 57.08 ATOM 2533 OG SER 374 42.301 42.578 -12.055 1.00 68.67 ATOM 2534 C SER 374 38.735 42.392 -11.070 1.00 53.37 ATOM 2535 O SER 374 38.358 42.931 -10.033 1.00 53.57 ATOM 2536 N LYS 375 37.954 42.204 -12.130 1.00 53.62 ATOM 2537 CA LYS 375 36.565 42.646 -12.165 1.00 54.04 ATOM 2538 CB LYS 375 35.804 41.962 -13.309 1.00 61.15 ATOM 2539 CG LYS 375 35.604 40.453 -13.172 1.00 71.46 ATOM 2540 CD LYS 375 34.757 39.912 -14.328 1.00 80.46 ATOM 2541 CE LYS 375 34.547 38.401 -14.234 1.00 85.39 ATOM 2542 NZ LYS 375 33.824 37.872 -15.438 1.00 89.61 ATOM 2543 C LYS 375 35.869 42.386 -10.847 1.00 49.20 ATOM 2544 O LYS 375 35.898 41.276 -10.352 1.00 49.05 ATOM 2545 N THR 376 35.289 43.420 -10.255 1.00 45.64 ATOM 2546 CA THR 376 34.614 43.239 -8.991 1.00 43.45 ATOM 2547 CB THR 376 34.597 44.516 -8.122 1.00 47.21 ATOM 2548 OG1 THR 376 33.898 45.562 -8.803 1.00 50.56 ATOM 2549 CG2 THR 376 36.017 44.975 -7.798 1.00 48.78 ATOM 2550 C THR 376 33.207 42.747 -9.207 1.00 40.09 ATOM 2551 O THR 376 32.642 42.852 -10.300 1.00 35.92 ATOM 2552 N ILE 377 32.656 42.202 -8.137 1.00 37.93 ATOM 2553 CA ILE 377 31.326 41.653 -8.137 1.00 36.78 ATOM 2554 CB ILE 377 31.362 40.152 -7.774 1.00 34.83 ATOM 2555 CG2 ILE 377 29.980 39.533 -7.895 1.00 32.45 ATOM 2556 CG1 ILE 377 32.348 39.413 -8.684 1.00 32.69 ATOM 2557 CD1 ILE 377 32.748 38.041 -8.162 1.00 27.92 ATOM 2558 C ILE 377 30.563 42.415 -7.072 1.00 39.31 ATOM 2559 O ILE 377 30.962 42.435 -5.896 1.00 38.63 ATOM 2560 N THR 378 29.566 43.169 -7.519 1.00 41.06 ATOM 2561 CA THR 378 28.712 43.918 -6.616 1.00 40.06 ATOM 2562 CB THR 378 28.209 45.243 -7.226 1.00 38.28 ATOM 2563 OG1 THR 378 29.316 46.145 -7.396 1.00 43.42 ATOM 2564 CG2 THR 378 27.163 45.891 -6.308 1.00 36.99 ATOM 2565 C THR 378 27.536 42.999 -6.323 1.00 40.53 ATOM 2566 O THR 378 27.024 42.310 -7.214 1.00 42.82 ATOM 2567 N SER 379 27.153 42.959 -5.054 1.00 41.66 ATOM 2568 CA SER 379 26.057 42.122 -4.585 1.00 37.15 ATOM 2569 CB SER 379 26.315 41.774 -3.123 1.00 39.90 ATOM 2570 OG SER 379 26.357 42.971 -2.344 1.00 39.97 ATOM 2571 C SER 379 24.738 42.872 -4.640 1.00 34.85 ATOM 2572 O SER 379 24.689 44.089 -4.869 1.00 34.30 ATOM 2573 N PRO 380 23.638 42.148 -4.448 1.00 30.97 ATOM 2574 CD PRO 380 23.467 40.702 -4.256 1.00 30.83 ATOM 2575 CA PRO 380 22.355 42.837 -4.467 1.00 31.60 ATOM 2576 CB PRO 380 21.355 41.692 -4.253 1.00 33.86 ATOM 2577 CG PRO 380 22.064 40.484 -4.705 1.00 29.90 ATOM 2578 C PRO 380 22.365 43.725 -3.219 1.00 31.83 ATOM 2579 O PRO 380 23.212 43.544 -2.338 1.00 34.52 ATOM 2580 N PHE 381 21.469 44.700 -3.144 1.00 31.79 ATOM 2581 CA PHE 381 21.399 45.514 -1.940 1.00 30.64 ATOM 2582 CB PHE 381 20.547 46.761 -2.152 1.00 26.26 ATOM 2583 CG PHE 381 20.422 47.617 -0.932 1.00 24.77 ATOM 2584 CD1 PHE 381 21.530 48.333 -0.452 1.00 26.36 ATOM 2585 CD2 PHE 381 19.198 47.712 -0.258 1.00 21.71 ATOM 2586 CE1 PHE 381 21.431 49.137 0.684 1.00 25.19 ATOM 2587 CE2 PHE 381 19.073 48.501 0.872 1.00 21.85 ATOM 2588 CZ PHE 381 20.201 49.224 1.353 1.00 27.79 ATOM 2589 C PHE 381 20.751 44.613 -0.881 1.00 32.40 ATOM 2590 O PHE 381 19.861 43.801 -1.185 1.00 32.67 ATOM 2591 N TYR 382 21.225 44.746 0.351 1.00 34.10 ATOM 2592 CA TYR 382 20.732 43.974 1.485 1.00 30.09 ATOM 2593 CB TYR 382 21.890 43.185 2.083 1.00 22.37 ATOM 2594 CG TYR 382 22.562 42.226 1.140 1.00 15.64 ATOM 2595 CD1 TYR 382 23.940 42.249 0.959 1.00 19.25 ATOM 2596 CE1 TYR 382 24.576 41.299 0.181 1.00 17.01 ATOM 2597 CD2 TYR 382 21.835 41.237 0.501 1.00 21.74 ATOM 2598 CE2 TYR 382 22.457 40.278 -0.286 1.00 17.61 ATOM 2599 CZ TYR 382 23.822 40.315 -0.436 1.00 20.73 ATOM 2600 OH TYR 382 24.406 39.331 -1.176 1.00 22.81 ATOM 2601 C TYR 382 20.220 44.975 2.530 1.00 33.35 ATOM 2602 O TYR 382 20.899 45.969 2.818 1.00 34.99 ATOM 2603 N GLY 383 19.014 44.748 3.051 1.00 32.94 ATOM 2604 CA GLY 383 18.457 45.635 4.064 1.00 32.92 ATOM 2605 C GLY 383 17.707 46.853 3.548 1.00 35.30 ATOM 2606 O GLY 383 17.148 46.820 2.454 1.00 32.00 ATOM 2607 N ASP 384 17.694 47.916 4.354 1.00 34.45 ATOM 2608 CA ASP 384 17.015 49.159 4.027 1.00 33.27 ATOM 2609 CB ASP 384 16.294 49.698 5.241 1.00 36.97 ATOM 2610 CG ASP 384 14.987 49.003 5.484 1.00 41.84 ATOM 2611 OD1 ASP 384 14.110 49.050 4.590 1.00 48.37 ATOM 2612 OD2 ASP 384 14.828 48.418 6.568 1.00 42.67 ATOM 2613 C ASP 384 17.936 50.224 3.531 1.00 35.10 ATOM 2614 O ASP 384 19.068 50.319 3.998 1.00 34.64 ATOM 2615 N LYS 385 17.447 51.020 2.577 1.00 39.67 ATOM 2616 CA LYS 385 18.212 52.128 1.969 1.00 42.47 ATOM 2617 CB LYS 385 17.461 52.731 0.766 1.00 49.42 ATOM 2618 CG LYS 385 17.308 51.805 -0.432 1.00 57.29 ATOM 2619 CD LYS 385 18.609 51.672 -1.254 1.00 63.49 ATOM 2620 CE LYS 385 18.395 50.774 -2.495 1.00 67.56 ATOM 2621 NZ LYS 385 19.579 50.684 -3.406 1.00 67.31 ATOM 2622 C LYS 385 18.442 53.219 2.993 1.00 39.12 ATOM 2623 O LYS 385 17.573 53.470 3.838 1.00 43.51 ATOM 2624 N SER 386 19.559 53.931 2.901 1.00 34.02 ATOM 2625 CA SER 386 19.771 54.934 3.913 1.00 34.23 ATOM 2626 CB SER 386 21.246 55.265 4.156 1.00 27.24 ATOM 2627 OG SER 386 21.916 55.575 2.988 1.00 29.42 ATOM 2628 C SER 386 18.928 56.164 3.825 1.00 39.30 ATOM 2629 O SER 386 18.289 56.441 2.814 1.00 45.39 ATOM 2630 N THR 387 18.847 56.790 4.994 1.00 44.75 ATOM 2631 CA THR 387 18.126 58.011 5.334 1.00 43.08 ATOM 2632 CB THR 387 17.432 57.749 6.690 1.00 45.54 ATOM 2633 OG1 THR 387 16.146 57.160 6.456 1.00 51.56 ATOM 2634 CG2 THR 387 17.365 58.983 7.581 1.00 48.46 ATOM 2635 C THR 387 19.219 59.058 5.509 1.00 41.51 ATOM 2636 O THR 387 19.060 60.229 5.207 1.00 45.34 ATOM 2637 N GLU 388 20.372 58.578 5.945 1.00 39.65 ATOM 2638 CA GLU 388 21.510 59.408 6.192 1.00 40.13 ATOM 2639 CB GLU 388 22.079 58.996 7.537 1.00 42.68 ATOM 2640 CG GLU 388 21.079 59.112 8.646 1.00 46.20 ATOM 2641 CD GLU 388 20.744 60.555 8.979 1.00 51.34 ATOM 2642 OE1 GLU 388 21.607 61.454 8.749 1.00 48.83 ATOM 2643 OE2 GLU 388 19.615 60.789 9.496 1.00 54.12 ATOM 2644 C GLU 388 22.554 59.136 5.115 1.00 40.71 ATOM 2645 O GLU 388 22.342 58.275 4.252 1.00 39.83 ATOM 2646 N PRO 389 23.702 59.825 5.183 1.00 42.10 ATOM 2647 CD PRO 389 24.063 60.916 6.114 1.00 42.78 ATOM 2648 CA PRO 389 24.763 59.619 4.198 1.00 44.35 ATOM 2649 CB PRO 389 25.851 60.608 4.654 1.00 45.07 ATOM 2650 CG PRO 389 25.090 61.684 5.323 1.00 43.93 ATOM 2651 C PRO 389 25.311 58.169 4.187 1.00 45.36 ATOM 2652 O PRO 389 25.363 57.489 5.234 1.00 46.15 ATOM 2653 N VAL 390 25.717 57.715 3.003 1.00 42.43 ATOM 2654 CA VAL 390 26.286 56.379 2.838 1.00 39.18 ATOM 2655 CB VAL 390 26.062 55.818 1.444 1.00 33.17 ATOM 2656 CG1 VAL 390 24.593 55.549 1.257 1.00 35.38 ATOM 2657 CG2 VAL 390 26.586 56.788 0.395 1.00 35.87 ATOM 2658 C VAL 390 27.766 56.466 3.077 1.00 41.43 ATOM 2659 O VAL 390 28.384 57.471 2.713 1.00 42.32 ATOM 2660 N GLN 391 28.310 55.434 3.726 1.00 44.86 ATOM 2661 CA GLN 391 29.739 55.358 4.638 1.00 47.38 ATOM 2662 CB GLN 391 29.982 55.249 5.559 1.00 49.86 ATOM 2663 CG GLN 391 29.536 56.490 6.359 1.00 50.20 ATOM 2664 CD GLN 391 29.613 56.298 7.868 1.00 53.83 ATOM 2665 OE1 GLN 391 30.599 55.765 8.384 1.00 52.70 ATOM 2666 NE2 GLN 391 28.575 56.739 8.583 1.00 48.35 ATOM 2667 C GLN 391 30.334 54.159 3.299 1.00 45.72 ATOM 2668 O GLN 391 29.836 53.032 3.392 1.00 46.80 ATOM 2669 N LYS 392 31.412 54.420 2.571 1.00 44.47 ATOM 2670 CA LYS 392 32.071 53.407 1.774 1.00 40.66 ATOM 2671 CB LYS 392 32.196 53.911 0.335 1.00 42.32 ATOM 2672 CG LYS 392 32.828 52.947 -0.666 1.00 48.87 ATOM 2673 CD LYS 392 32.022 51.647 -0.844 1.00 51.56 ATOM 2674 CE LYS 392 32.284 50.967 -2.202 1.00 50.35 ATOM 2675 NZ LYS 392 31.718 51.738 -3.365 1.00 53.19 ATOM 2676 C LYS 392 33.439 53.116 2.328 1.00 38.02 ATOM 2677 O LYS 392 34.230 54.024 2.578 1.00 40.88 ATOM 2678 N LEU 393 33.692 51.839 2.562 1.00 35.52 ATOM 2679 CA LEU 393 34.978 51.395 3.052 1.00 33.95 ATOM 2680 CB LEU 393 34.827 50.700 4.404 1.00 30.25 ATOM 2681 CG LEU 393 34.497 51.594 5.596 1.00 30.20 ATOM 2682 CD1 LEU 393 34.535 50.778 6.890 1.00 32.88 ATOM 2683 CD2 LEU 393 35.506 52.722 5.664 1.00 31.84 ATOM 2684 C LEU 393 35.528 50.418 2.014 1.00 34.73 ATOM 2685 O LEU 393 34.796 49.539 1.543 1.00 36.19 ATOM 2686 N SER 394 36.780 50.620 1.614 1.00 31.82 ATOM 2687 CA SER 394 37.430 49.747 0.652 1.00 37.44 ATOM 2688 CB SER 394 37.971 50.516 -0.541 1.00 41.95 ATOM 2689 OG SER 394 38.489 49.617 -1.521 1.00 50.00 ATOM 2690 C SER 394 38.591 49.051 1.312 1.00 39.64 ATOM 2691 O SER 394 39.512 49.695 1.835 1.00 42.33 ATOM 2692 N PHE 395 38.567 47.733 1.248 1.00 37.33 ATOM 2693 CA PHE 395 39.605 46.933 1.846 1.00 39.32 ATOM 2694 CB PHE 395 38.963 45.836 2.682 1.00 34.54 ATOM 2695 CG PHE 395 37.909 46.337 3.615 1.00 32.96 ATOM 2696 CD1 PHE 395 36.563 46.226 3.278 1.00 25.90 ATOM 2697 CD2 PHE 395 38.258 46.916 4.835 1.00 30.10 ATOM 2698 CE1 PHE 395 35.575 46.678 4.138 1.00 25.06 ATOM 2699 CE2 PHE 395 37.270 47.376 5.708 1.00 31.10 ATOM 2700 CZ PHE 395 35.921 47.255 5.356 1.00 27.26 ATOM 2701 C PHE 395 40.555 46.333 0.818 1.00 42.66 ATOM 2702 O PHE 395 41.275 45.388 1.127 1.00 43.59 ATOM 2703 N ASP 396 40.544 46.858 -0.404 1.00 44.49 ATOM 2704 CA ASP 396 41.434 46.355 -1.449 1.00 46.90 ATOM 2705 CB ASP 396 41.338 47.261 -2.693 1.00 49.42 ATOM 2706 CG ASP 396 42.396 46.935 -3.764 1.00 55.28 ATOM 2707 OD1 ASP 396 42.247 45.919 -4.494 1.00 54.98 ATOM 2708 OD2 ASP 396 43.374 47.717 -3.884 1.00 56.58 ATOM 2709 C ASP 396 42.879 46.293 -0.914 1.00 48.42 ATOM 2710 O ASP 396 43.417 47.308 -0.452 1.00 51.13 ATOM 2711 N GLY 397 43.465 45.093 -0.908 1.00 47.37 ATOM 2712 CA GLY 397 44.836 44.908 -0.437 1.00 49.02 ATOM 2713 C GLY 397 45.040 44.597 1.045 1.00 49.20 ATOM 2714 O GLY 397 46.155 44.290 1.497 1.00 50.80 ATOM 2715 N GLN 398 43.949 44.642 1.797 1.00 48.76 ATOM 2716 CA GLN 398 43.973 44.402 3.229 1.00 43.09 ATOM 2717 CB GLN 398 43.194 45.515 3.957 1.00 42.33 ATOM 2718 CG GLN 398 43.622 46.937 3.625 1.00 40.39 ATOM 2719 CD GLN 398 45.056 47.224 4.023 1.00 41.78 ATOM 2720 OE1 GLN 398 45.473 46.965 5.149 1.00 40.33 ATOM 2721 NE2 GLN 398 45.827 47.747 3.088 1.00 46.48 ATOM 2722 C GLN 398 43.353 43.051 3.576 1.00 39.37 ATOM 2723 O GLN 398 42.579 42.480 2.793 1.00 35.23 ATOM 2724 N LYS 399 43.741 42.535 4.740 1.00 36.01 ATOM 2725 CA LYS 399 43.220 41.283 5.271 1.00 32.45 ATOM 2726 CB LYS 399 44.354 40.298 5.627 1.00 32.95 ATOM 2727 CG LYS 399 45.153 39.758 4.467 1.00 35.89 ATOM 2728 CD LYS 399 44.318 38.913 3.525 1.00 45.68 ATOM 2729 CE LYS 399 45.157 38.442 2.309 1.00 55.14 ATOM 2730 NZ LYS 399 44.438 37.617 1.261 1.00 52.03 ATOM 2731 C LYS 399 42.506 41.712 6.558 1.00 28.99 ATOM 2732 O LYS 399 43.163 42.099 7.528 1.00 27.89 ATOM 2733 N VAL 400 41.178 41.713 6.547 1.00 21.30 ATOM 2734 CA VAL 400 40.433 42.091 7.736 1.00 22.51 ATOM 2735 CB VAL 400 39.005 42.610 7.399 1.00 23.45 ATOM 2736 CG1 VAL 400 38.225 42.938 8.675 1.00 17.30 ATOM 2737 CG2 VAL 400 39.120 43.846 6.543 1.00 22.17 ATOM 2738 C VAL 400 40.385 40.895 8.666 1.00 20.47 ATOM 2739 O VAL 400 39.623 39.965 8.464 1.00 20.32 ATOM 2740 N TYR 401 41.177 40.946 9.718 1.00 22.08 ATOM 2741 CA TYR 401 41.235 39.832 10.626 1.00 23.87 ATOM 2742 CB TYR 401 42.686 39.513 10.967 1.00 23.92 ATOM 2743 CG TYR 401 43.399 40.624 11.667 1.00 21.62 ATOM 2744 CD1 TYR 401 43.361 40.718 13.049 1.00 23.62 ATOM 2745 CE1 TYR 401 44.024 41.725 13.718 1.00 22.25 ATOM 2746 CD2 TYR 401 44.124 41.583 10.949 1.00 23.09 ATOM 2747 CE2 TYR 401 44.791 42.607 11.602 1.00 21.21 ATOM 2748 CZ TYR 401 44.733 42.663 12.995 1.00 26.42 ATOM 2749 OH TYR 401 45.392 43.644 13.698 1.00 38.32 ATOM 2750 C TYR 401 40.421 39.971 11.886 1.00 25.97 ATOM 2751 O TYR 401 40.523 39.117 12.762 1.00 24.72 ATOM 2752 N ARG 402 39.627 41.033 11.999 1.00 25.45 ATOM 2753 CA ARG 402 38.797 41.206 13.181 1.00 21.27 ATOM 2754 CB ARG 402 39.671 41.438 14.397 1.00 20.74 ATOM 2755 CG ARG 402 38.922 41.510 15.687 1.00 19.16 ATOM 2756 CD ARG 402 39.831 42.048 16.720 1.00 16.61 ATOM 2757 NE ARG 402 39.323 41.788 18.050 1.00 24.94 ATOM 2758 CZ ARG 402 40.054 41.922 19.154 1.00 34.52 ATOM 2759 NH1 ARG 402 39.521 41.650 20.337 1.00 40.04 ATOM 2760 NH2 ARG 402 41.314 42.347 19.081 1.00 29.20 ATOM 2761 C ARG 402 37.794 42.340 13.079 1.00 22.04 ATOM 2762 O ARG 402 38.103 43.401 12.539 1.00 21.07 ATOM 2763 N THR 403 36.622 42.113 13.670 1.00 23.72 ATOM 2764 CA THR 403 35.519 43.062 13.702 1.00 22.58 ATOM 2765 CB THR 403 34.395 42.681 12.701 1.00 26.34 ATOM 2766 OG1 THR 403 33.865 41.394 13.027 1.00 31.05 ATOM 2767 CG2 THR 403 34.930 42.618 11.297 1.00 28.24 ATOM 2768 C THR 403 34.942 43.074 15.111 1.00 19.93 ATOM 2769 O THR 403 34.810 42.033 15.751 1.00 17.31 ATOM 2770 N ILE 404 34.672 44.274 15.603 1.00 21.50 ATOM 2771 CA ILE 404 34.117 44.490 16.941 1.00 23.42 ATOM 2772 CB ILE 404 35.139 45.177 17.888 1.00 22.26 ATOM 2773 CG2 ILE 404 34.511 45.385 19.290 1.00 25.17 ATOM 2774 CG1 ILE 404 36.436 44.355 17.945 1.00 19.77 ATOM 2775 CD1 ILE 404 37.514 44.953 18.807 1.00 19.18 ATOM 2776 C ILE 404 32.952 45.431 16.738 1.00 22.13 ATOM 2777 O ILE 404 33.123 46.554 16.251 1.00 20.52 ATOM 2778 N ALA 405 31.769 44.967 17.091 1.00 24.23 ATOM 2779 CA ALA 405 30.566 45.761 16.903 1.00 29.85 ATOM 2780 CB ALA 405 29.505 44.951 16.164 1.00 32.90 ATOM 2781 C ALA 405 29.998 46.268 18.196 1.00 30.65 ATOM 2782 O ALA 405 30.172 45.654 19.261 1.00 32.26 ATOM 2783 N ASN 406 29.314 47.401 18.086 1.00 33.60 ATOM 2784 CA ASN 406 28.657 48.036 19.213 1.00 30.90 ATOM 2785 CB ASN 406 29.353 49.328 19.575 1.00 35.26 ATOM 2786 CG ASN 406 30.688 49.082 20.251 1.00 39.28 ATOM 2787 OD1 ASN 406 31.716 49.567 19.796 1.00 46.28 ATOM 2788 ND2 ASN 406 30.677 48.323 21.345 1.00 41.47 ATOM 2789 C ASN 406 27.221 48.255 18.823 1.00 27.42 ATOM 2790 O ASN 406 26.917 48.549 17.680 1.00 31.60 ATOM 2791 N THR 407 26.335 48.093 19.779 1.00 28.95 ATOM 2792 CA THR 407 24.923 48.210 19.527 1.00 27.59 ATOM 2793 CB THR 407 24.307 46.799 19.792 1.00 29.44 ATOM 2794 OG1 THR 407 23.752 46.264 18.585 1.00 34.58 ATOM 2795 CG2 THR 407 23.274 46.801 20.891 1.00 32.65 ATOM 2796 C THR 407 24.312 49.344 20.376 1.00 29.05 ATOM 2797 O THR 407 25.039 50.103 21.043 1.00 29.87 ATOM 2798 N ASP 408 22.994 49.517 20.272 1.00 30.18 ATOM 2799 CA ASP 408 22.248 50.520 21.040 1.00 26.65 ATOM 2800 CB ASP 408 22.396 51.893 20.417 1.00 26.06 ATOM 2801 CG ASP 408 22.171 53.004 21.396 1.00 28.54 ATOM 2802 OD1 ASP 408 22.823 54.054 21.232 1.00 32.74 ATOM 2803 OD2 ASP 408 21.362 52.841 22.322 1.00 22.44 ATOM 2804 C ASP 408 20.777 50.102 21.089 1.00 25.70 ATOM 2805 O ASP 408 20.375 49.156 20.412 1.00 26.95 ATOM 2806 N VAL 409 19.998 50.740 21.949 1.00 26.74 ATOM 2807 CA VAL 409 18.579 50.416 22.096 1.00 29.52 ATOM 2808 CB VAL 409 18.318 49.460 23.308 1.00 33.88 ATOM 2809 CG1 VAL 409 18.152 48.015 22.865 1.00 32.06 ATOM 2810 CG2 VAL 409 19.450 49.583 24.330 1.00 36.32 ATOM 2811 C VAL 409 17.750 51.675 22.354 1.00 29.41 ATOM 2812 O VAL 409 18.284 52.726 22.744 1.00 27.31 ATOM 2813 N ALA 410 16.438 51.524 22.174 1.00 28.05 ATOM 2814 CA ALA 410 15.450 52.573 22.397 1.00 21.88 ATOM 2815 CB ALA 410 15.244 53.387 21.135 1.00 18.08 ATOM 2816 C ALA 410 14.196 51.772 22.734 1.00 22.70 ATOM 2817 O ALA 410 13.674 51.018 21.905 1.00 19.65 ATOM 2818 N ALA 411 13.805 51.820 24.003 1.00 27.52 ATOM 2819 CA ALA 411 12.623 51.091 24.470 1.00 31.81 ATOM 2820 CB ALA 411 12.873 50.502 25.829 1.00 33.93 ATOM 2821 C ALA 411 11.431 52.029 24.525 1.00 34.20 ATOM 2822 O ALA 411 11.535 53.147 25.038 1.00 34.95 ATOM 2823 N TRP 412 10.306 51.592 23.987 1.00 33.77 ATOM 2824 CA TRP 412 9.134 52.436 23.996 1.00 39.98 ATOM 2825 CB TRP 412 8.392 52.358 22.669 1.00 41.61 ATOM 2826 CG TRP 412 9.054 53.098 21.571 1.00 43.46 ATOM 2827 CD2 TRP 412 8.430 53.596 20.392 1.00 45.56 ATOM 2828 CE2 TRP 412 9.440 54.195 19.607 1.00 42.47 ATOM 2829 CE3 TRP 412 7.110 53.590 19.916 1.00 46.54 ATOM 2830 CD1 TRP 412 10.376 53.412 21.467 1.00 44.40 ATOM 2831 NE1 TRP 412 10.617 54.067 20.288 1.00 43.38 ATOM 2832 CZ2 TRP 412 9.177 54.788 18.377 1.00 45.51 ATOM 2833 CZ3 TRP 412 6.844 54.179 18.689 1.00 46.75 ATOM 2834 CH2 TRP 412 7.877 54.770 17.931 1.00 48.56 ATOM 2835 C TRP 412 8.213 52.038 25.114 1.00 44.25 ATOM 2836 O TRP 412 8.109 50.853 25.444 1.00 42.52 ATOM 2837 N PRO 413 7.519 53.028 25.716 1.00 50.07 ATOM 2838 CD PRO 413 7.624 54.477 25.453 1.00 50.83 ATOM 2839 CA PRO 413 6.584 52.781 26.815 1.00 50.92 ATOM 2840 CB PRO 413 5.903 54.138 26.979 1.00 50.26 ATOM 2841 CG PRO 413 7.019 55.079 26.697 1.00 49.66 ATOM 2842 C PRO 413 5.599 51.690 26.424 1.00 51.13 ATOM 2843 O PRO 413 5.244 50.846 27.240 1.00 53.47 ATOM 2844 N ASN 414 5.227 51.674 25.148 1.00 52.31 ATOM 2845 CA ASN 414 4.291 50.687 24.624 1.00 54.17 ATOM 2846 CB ASN 414 3.559 51.238 23.388 1.00 58.82 ATOM 2847 CG ASN 414 4.490 51.960 22.411 1.00 61.33 ATOM 2848 OD1 ASN 414 4.680 53.184 22.501 1.00 64.05 ATOM 2849 ND2 ASN 414 5.073 51.210 21.480 1.00 55.75 ATOM 2850 C ASN 414 4.947 49.338 24.321 1.00 54.03 ATOM 2851 O ASN 414 4.481 48.586 23.466 1.00 55.84 ATOM 2852 N GLY 415 6.058 49.060 24.992 1.00 51.36 ATdM 2853 CA GLY 415 6.737 47.792 24.811 1.00 50.33 ATOM 2854 C GLY 415 7.639 47.544 23.614 1.00 49.60 ATOM 2855 O GLY 415 8.402 46.582 23.616 1.00 55.05 ATOM 2856 N LYS 416 7.578 48.375 22.591 1.00 46.50 ATOM 2857 CA LYS 416 8.423 48.147 21.431 1.00 43.10 ATOM 2858 CB LYS 416 7.982 49.065 20.294 1.00 45.88 ATOM 2859 CG LYS 416 6.489 49.015 19.988 1.00 48.22 ATOM 2860 CD LYS 416 6.139 47.815 19.142 1.00 53.88 ATOM 2861 CE LYS 416 4.658 47.762 18.779 1.00 53.22 ATOM 2862 NZ LYS 416 4.374 46.692 17.766 1.00 54.21 ATOM 2863 C LYS 416 9.887 48.429 21.775 1.00 39.40 ATOM 2864 O LYS 416 10.197 49.492 22.311 1.00 39.18 ATOM 2865 N VAL 417 10.771 47.453 21.571 1.00 36.07 ATOM 2866 CA VAL 417 12.198 47.682 21.818 1.00 33.10 ATOM 2867 CB VAL 417 12.851 46.648 22.748 1.00 32.27 ATOM 2868 CG1 VAL 417 14.357 46.934 22.860 1.00 29.20 ATOM 2869 CG2 VAL 417 12.234 46.738 24.127 1.00 30.38 ATOM 2870 C VAL 417 12.893 47.682 20.469 1.00 33.32 ATOM 2871 O VAL 417 12.521 46.923 19.558 1.00 32.49 ATOM 2872 N TYR 418 13.877 48.562 20.332 1.00 32.46 ATOM 2873 CA TYR 418 14.584 48.700 19.078 1.00 30.70 ATOM 2874 CB TYR 418 14.201 50.034 18.430 1.00 35.09 ATOM 2875 CG TYR 418 12.723 50.142 18.087 1.00 39.67 ATOM 2876 CD1 TYR 418 11.830 50.796 18.939 1.00 41.36 ATOM 2877 CE1 TYR 418 10.468 50.837 18.656 1.00 41.55 ATOM 2878 CD2 TYR 418 12.210 49.539 16.938 1.00 42.74 ATOM 2879 CE2 TYR 418 10.858 49.579 16.649 1.00 41.49 ATOM 2880 CZ TYR 418 9.997 50.224 17.512 1.00 40.58 ATOM 2881 OH TYR 418 8.660 50.227 17.231 1.00 43.39 ATOM 2882 C TYR 418 16.087 48.604 19.217 1.00 31.90 ATOM 2883 O TYR 418 16.674 49.292 20.050 1.00 34.09 ATOM 2884 N LEU 419 16.697 47.794 18.349 1.00 35.53 ATOM 2885 CA LEU 419 18.145 47.575 18.313 1.00 35.73 ATOM 2886 CB LEU 419 18.470 46.188 18.875 1.00 40.81 ATOM 2887 CG LEU 419 18.374 46.005 20.396 1.00 45.56 ATOM 2888 CD1 LEU 419 17.661 44.692 20.771 1.00 47.76 ATOM 2889 CD2 LEU 419 19.783 46.064 20.993 1.00 47.90 ATOM 2890 C LEU 419 18.739 47.717 16.898 1.00 34.04 ATOM 2891 O LEU 419 18.017 47.650 15.889 1.00 34.32 ATOM 2892 N GLY 420 20.049 47.940 16.841 1.00 29.29 ATOM 2893 CA GLY 420 20.743 48.085 15.576 1.00 26.65 ATOM 2894 C GLY 420 22.211 48.353 15.836 1.00 27.14 ATOM 2895 O GLY 420 22.575 48.680 16.964 1.00 28.38 ATOM 2896 N VAL 421 23.046 48.253 14.803 1.00 26.69 ATOM 2897 CA VAL 421 24.490 48.452 14.924 1.00 24.73 ATOM 2898 CB VAL 421 25.274 47.527 13.945 1.00 26.82 ATOM 2899 CG1 VAL 421 26.784 47.789 14.031 1.00 25.39 ATOM 2900 CG2 VAL 421 24.993 46.080 14.252 1.00 23.09 ATOM 2901 C VAL 421 24.878 49.893 14.640 1.00 27.15 ATOM 2902 O VAL 421 24.661 50.401 13.539 1.00 30.83 ATOM 2903 N THR 422 25.535 50.521 15.606 1.00 27.69 ATOM 2904 CA THR 422 25.946 51.910 15.470 1.00 28.13 ATOM 2905 CB THR 422 25.717 52.692 16.789 1.00 27.76 ATOM 2906 OG1 THR 422 26.642 52.239 17.782 1.00 26.20 ATOM 2907 CG2 THR 422 24.285 52.503 17.289 1.00 22.77 ATOM 2908 C THR 422 27.414 52.047 15.133 1.00 29.17 ATOM 2909 O THR 422 27.864 53.111 14.726 1.00 31.06 ATOM 2910 N LYS 423 28.167 50.974 15.315 1.00 31.17 ATOM 2911 CA LYS 423 29.591 51.032 15.079 1.00 30.80 ATOM 2912 CB LYS 423 30.242 51.794 16.234 1.00 27.04 ATOM 2913 CG LYS 423 31.689 52.148 16.020 1.00 27.11 ATOM 2914 CD LYS 423 32.186 52.755 17.273 1.00 31.47 ATOM 2915 CE LYS 423 33.668 52.750 17.356 1.00 32.44 ATOM 2916 NZ LYS 423 33.955 53.029 18.792 1.00 43.38 ATOM 2917 C LYS 423 30.247 49.662 14.914 1.00 31.76 ATOM 2918 O LYS 423 29.828 48.662 15.529 1.00 32.10 ATOM 2919 N VAL 424 31.240 49.629 14.026 1.00 31.62 ATOM 2920 CA VAL 424 32.015 48.435 13.715 1.00 30.00 ATOM 2921 CB VAL 424 31.408 47.626 12.543 1.00 26.10 ATOM 2922 CG1 VAL 424 32.157 46.316 12.382 1.00 24.90 ATOM 2923 CG2 VAL 424 29.915 47.367 12.769 1.00 23.72 ATOM 2924 C VAL 424 33.430 48.856 13.329 1.00 29.28 ATOM 2925 O VAL 424 33.622 49.766 12.524 1.00 29.28 ATOM 2926 N ASP 425 34.409 48.247 13.984 1.00 32.53 ATOM 2927 CA ASP 425 35.816 48.508 13.720 1.00 32.64 ATOM 2928 CB ASP 425 36.598 48.641 15.021 1.00 34.95 ATOM 2929 CG ASP 425 36.257 49.900 15.769 1.00 45.99 ATOM 2930 OD1 ASP 425 36.132 50.961 15.117 1.00 46.60 ATOM 2931 OD2 ASP 425 36.107 49.828 17.010 1.00 52.51 ATOM 2932 C ASP 425 36.369 47.329 12.954 1.00 30.71 ATOM 2933 O ASP 425 36.189 46.176 13.364 1.00 28.66 ATOM 2934 N PHE 426 37.035 47.619 11.845 1.00 30.44 ATOM 2935 CA PHE 426 37.641 46.599 11.003 1.00 27.35 ATOM 2936 CB PHE 426 37.265 46.824 9.533 1.00 23.83 ATOM 2937 CG PHE 426 35.811 46.617 9.260 1.00 22.42 ATOM 2938 CD1 PHE 426 34.917 47.675 9.353 1.00 29.21 ATOM 2939 CD2 PHE 426 35.325 45.356 8.952 1.00 23.84 ATOM 2940 CE1 PHE 426 33.535 47.482 9.143 1.00 30.42 ATOM 2941 CE2 PHE 426 33.953 45.141 8.738 1.00 28.45 ATOM 2942 CZ PHE 426 33.054 46.211 8.836 1.00 25.84 ATOM 2943 C PHE 426 39.143 46.651 11.169 1.00 27.60 ATOM 2944 O PHE 426 39.764 47.605 10.719 1.00 30.18 ATOM 2945 N SER 427 39.704 45.697 11.914 1.00 28.92 ATOM 2946 CA SER 427 41.159 45.613 12.097 1.00 31.13 ATOM 2947 CB SER 427 41.527 44.834 13.354 1.00 23.47 ATOM 2948 OG SER 427 41.323 45.630 14.488 1.00 34.58 ATOM 2949 C SER 427 41.734 44.896 10.885 1.00 30.97 ATOM 2950 O SER 427 41.582 43.678 10.741 1.00 34.75 ATOM 2951 N GLN 428 42.388 45.647 10.019 1.00 32.50 ATOM 2952 CA GLN 428 42.943 45.068 8.819 1.00 34.39 ATOM 2953 CB GLN 428 42.474 45.849 7.597 1.00 35.19 ATOM 2954 CG GLN 428 42.655 47.358 7.703 1.00 36.26 ATOM 2955 CD GLN 428 41.875 48.109 6.636 1.00 37.21 ATOM 2956 OE1 GLN 428 40.922 47.576 6.041 1.00 37.62 ATOM 2957 NE2 GLN 428 42.263 49.357 6.395 1.00 37.30 ATOM 2958 C GLN 428 44.445 45.024 8.895 1.00 34.53 ATOM 2959 O GLN 428 45.047 45.761 9.658 1.00 32.24 ATOM 2960 N TYR 429 45.026 44.081 8.168 1.00 39.80 ATOM 2961 CA TYR 429 46.465 43.909 8.113 1.00 43.52 ATOM 2962 CB TYR 429 46.867 42.578 8.733 1.00 45.24 ATOM 2963 CG TYR 429 48.340 42.256 8.618 1.00 44.33 ATOM 2964 CD1 TYR 429 49.285 42.965 9.350 1.00 44.13 ATOM 2965 CE1 TYR 429 50.647 42.652 9.270 1.00 46.61 ATOM 2966 CD2 TYR 429 48.784 41.222 7.794 1.00 45.15 ATOM 2967 CE2 TYR 429 50.135 40.897 7.709 1.00 48.28 ATOM 2968 CZ TYR 429 51.064 41.614 8.451 1.00 48.90 ATOM 2969 OH TYR 429 52.400 41.271 8.405 1.00 49.66 ATOM 2970 C TYR 429 46.905 43.961 6.653 1.00 48.69 ATOM 2971 O TYR 429 46.203 43.476 5.759 1.00 46.50 ATOM 2972 N ASP 430 48.069 44.560 6.431 1.00 54.63 ATOM 2973 CA ASP 430 48.649 44.716 5.112 1.00 58.67 ATOM 2974 CB ASP 430 49.064 46.175 4.942 1.00 58.82 ATOM 2975 CG ASP 430 49.474 46.522 3.518 1.00 63.70 ATOM 2976 OD1 ASP 430 49.781 45.612 2.709 1.00 62.99 ATOM 2977 OD2 ASP 430 49.494 47.737 3.211 1.00 65.11 ATOM 2978 C ASP 430 49.874 43.798 5.015 1.00 63.15 ATOM 2979 O ASP 430 50.820 43.932 5.790 1.00 62.58 ATOM 2980 N ASP 431 49.846 42.865 4.065 1.00 69.35 ATOM 2981 CA ASP 431 50.951 41.916 3.852 1.00 74.25 ATOM 2982 CB ASP 431 50.578 40.849 2.802 1.00 78.72 ATOM 2983 CG ASP 431 49.404 39.965 3.231 1.00 83.39 ATOM 2984 OD1 ASP 431 49.588 39.108 4.127 1.00 86.73 ATOM 2985 OD2 ASP 431 48.299 40.117 2.657 1.00 85.57 ATOM 2986 C ASP 431 52.189 42.659 3.365 1.00 74.94 ATOM 2987 O ASP 431 53.265 42.526 3.937 1.00 74.05 ATOM 2988 N GLN 432 52.006 43.437 2.300 1.00 77.50 ATOM 2989 CA GLN 432 53.067 44.230 1.683 1.00 78.85 ATOM 2990 CB GLN 432 52.469 45.250 0.709 1.00 84.24 ATOM 2991 CG GLN 432 52.081 44.770 -0.664 1.00 94.21 ATOM 2992 CD GLN 432 51.874 45.945 -1.635 1.00 101.21 ATOM 2993 OE1 GLN 432 51.963 45.777 -2.856 1.00 102.84 ATOM 2994 NE2 GLN 432 51.620 47.141 -1.092 1.00 103.92 ATOM 2995 C GLN 432 53.875 45.043 2.683 1.00 76.88 ATOM 2996 O GLN 432 55.015 44.727 3.020 1.00 75.05 ATOM 2997 N LYS 433 53.245 46.122 3.122 1.00 74.75 ATOM 2998 CA LYS 433 53.841 47.075 4.032 1.00 73.23 ATOM 2999 CB LYS 433 53.030 48.372 3.965 1.00 77.09 ATOM 3000 CG LYS 433 52.809 48.809 2.501 1.00 82.48 ATOM 3001 CD LYS 433 51.969 50.069 2.321 1.00 85.49 ATOM 3002 CE LYS 433 51.789 50.363 0.828 1.00 85.34 ATOM 3003 NZ LYS 433 51.088 51.648 0.574 1.00 83.39 ATOM 3004 C LYS 433 53.983 46.549 5.446 1.00 70.28 ATOM 3005 O LYS 433 54.678 47.139 6.266 1.00 69.41 ATOM 3006 N ASN 434 53.359 45.409 5.711 1.00 70.07 ATOM 3007 CA ASN 434 53.424 44.788 7.026 1.00 69.13 ATOM 3008 CB ASN 434 54.833 44.269 7.292 1.00 72.41 ATOM 3009 CG ASN 434 54.838 43.081 8.213 1.00 77.33 ATOM 3010 OD1 ASN 434 54.802 43.220 9.436 1.00 80.62 ATOM 3011 ND2 ASN 434 54.833 41.892 7.631 1.00 82.09 ATOM 3012 C ASN 434 53.018 45.790 8.099 1.00 66.04 ATOM 3013 O ASN 434 53.745 46.042 9.055 1.00 66.81 ATOM 3014 N GLU 435 51.862 46.399 7.896 1.00 63.11 ATOM 3015 CA GLU 435 51.339 47.376 8.828 1.00 60.05 ATOM 3016 CB GLU 435 51.279 48.762 8.171 1.00 65.39 ATOM 3017 CG GLU 435 50.404 48.827 6.908 1.00 71.11 ATOM 3018 CD GLU 435 50.166 50.249 6.398 1.00 76.12 ATOM 3019 OE1 GLU 435 51.151 50.987 6.158 1.00 77.71 ATOM 3020 OE2 GLU 435 48.985 50.623 6.221 1.00 76.57 ATOM 3021 C GLU 435 49.933 46.940 9.207 1.00 56.46 ATOM 3022 O GLU 435 49.271 46.226 8.443 1.00 53.33 ATOM 3023 N THR 436 49.513 47.310 10.412 1.00 52.67 ATOM 3024 CA THR 436 48.172 47.011 10.889 1.00 48.22 ATOM 3025 CB THR 436 48.180 46.265 12.243 1.00 49.49 ATOM 3026 OG1 THR 436 48.928 47.011 13.217 1.00 53.64 ATOM 3027 CG2 THR 436 48.786 44.882 12.074 1.00 50.64 ATOM 3028 C THR 436 47.473 48.358 11.032 1.00 44.20 ATOM 3029 O THR 436 48.120 49.373 11.308 1.00 43.15 ATOM 3030 N SER 437 46.172 48.383 10.784 1.00 39.81 ATOM 3031 CA SER 437 45.404 49.610 10.876 1.00 35.83 ATOM 3032 CB SER 437 45.525 50.401 9.567 1.00 34.84 ATOM 3033 OG SER 437 45.215 49.603 8.430 1.00 26.92 ATOM 3034 C SER 437 43.954 49.262 11.147 1.00 38.35 ATOM 3035 O SER 437 43.571 48.082 11.142 1.00 40.79 ATOM 3036 N THR 438 43.138 50.288 11.354 1.00 37.88 ATOM 3037 CA THR 438 41.723 50.088 11.618 1.00 31.21 ATOM 3038 CB THR 438 41.421 50.443 13.091 1.00 30.02 ATOM 3039 OG1 THR 438 42.206 49.607 13.943 1.00 33.35 ATOM 3040 CG2 THR 438 39.981 50.224 13.428 1.00 32.55 ATOM 3041 C THR 438 40.909 50.974 10.672 1.00 31.00 ATOM 3042 O THR 438 41.434 51.916 10.084 1.00 31.16 ATOM 3043 N GLU 439 39.676 50.576 10.416 1.00 30.22 ATOM 3044 CA GLU 439 38.768 51.358 9.602 1.00 34.37 ATOM 3045 CB GLU 439 38.611 50.789 8.204 1.00 40.27 ATOM 3046 CG GLU 439 39.717 51.176 7.242 1.00 42.06 ATOM 3047 CD GLU 439 39.296 50.989 5.805 1.00 40.04 ATOM 3048 OE1 GLU 439 39.526 49.892 5.232 1.00 36.27 ATOM 3049 OE2 GLU 439 38.711 51.952 5.267 1.00 39.88 ATOM 3050 C GLU 439 37.478 51.222 10.377 1.00 37.64 ATOM 3051 O GLU 439 37.216 50.158 10.948 1.00 39.86 ATOM 3052 N THR 440 36.614 52.224 10.297 1.00 37.34 ATOM 3053 CA THR 440 35.409 52.209 11.108 1.00 34.42 ATOM 3054 CB THR 440 35.649 53.180 12.268 1.00 35.98 ATOM 3055 OG1 THR 440 36.922 52.904 12.871 1.00 36.26 ATOM 3056 CG2 THR 440 34.523 53.111 13.294 1.00 40.16 ATOM 3057 C THR 440 34.076 52.624 10.496 1.00 33.02 ATOM 3058 O THR 440 34.012 53.522 9.668 1.00 32.99 ATOM 3059 N TYR 441 33.005 51.984 10.947 1.00 34.71 ATOM 3060 CA TYR 441 31.664 52.382 10.548 1.00 32.57 ATOM 3061 CB TYR 441 30.798 51.202 10.102 1.00 30.07 ATOM 3062 CG TYR 441 29.315 51.543 10.127 1.00 30.12 ATOM 3063 CD1 TYR 441 28.777 52.454 9.222 1.00 28.88 ATOM 3064 CE1 TYR 441 27.456 52.877 9.325 1.00 29.33 ATOM 3065 CD2 TYR 441 28.478 51.046 11.135 1.00 29.87 ATOM 3066 CE2 TYR 441 27.164 51.462 11.245 1.00 27.38 ATOM 3067 CZ TYR 441 26.660 52.384 10.337 1.00 29.54 ATOM 3068 OH TYR 441 25.372 52.851 10.468 1.00 30.14 ATOM 3069 C TYR 441 31.047 52.990 11.815 1.00 34.37 ATOM 3070 O TYR 441 30.872 52.289 12.802 1.00 33.76 ATOM 3071 N ASP 442 30.749 54.286 11.791 1.00 35.80 ATOM 3072 CA ASP 442 30.131 54.987 12.915 1.00 36.42 ATOM 3073 CB ASP 442 31.069 56.096 13.429 1.00 42.66 ATOM 3074 CG ASP 442 30.795 56.488 14.897 1.00 48.14 ATOM 3075 OD1 ASP 442 29.611 56.518 15.319 1.00 50.77 ATOM 3076 OD2 ASP 442 31.775 56.770 15.630 1.00 49.26 ATOM 3077 C ASP 442 28.834 55.595 12.371 1.00 38.05 ATOM 3078 O ASP 442 28.861 56.412 11.451 1.00 37.61 ATOM 3079 N SER 443 27.694 55.195 12.924 1.00 39.24 ATOM 3080 CA SER 443 26.406 55.697 12.456 1.00 40.93 ATOM 3081 CB SER 443 25.257 54.972 13.146 1.00 43.62 ATOM 3082 OG SER 443 25.233 55.289 14.529 1.00 44.57 ATOM 3083 C SER 443 26.289 57.180 12.714 1.00 42.03 ATOM 3084 O SER 443 25.411 57.851 12.174 1.00 39.08 ATOM 3085 N LYS 444 27.130 57.661 13.620 1.00 46.56 ATOM 3086 CA LYS 444 27.179 59.063 13.977 1.00 51.18 ATOM 3087 CB LYS 444 27.357 59.894 12.706 1.00 53.90 ATOM 3088 CG LYS 444 28.579 59.425 11.922 1.00 62.90 ATOM 3089 CD LYS 444 28.719 60.075 10.563 1.00 73.49 ATOM 3090 CE LYS 444 30.022 59.640 9.895 1.00 77.94 ATOM 3091 NZ LYS 444 30.378 60.504 8.729 1.00 84.38 ATOM 3092 C LYS 444 26.062 59.589 14.892 1.00 51.23 ATOM 3093 O LYS 444 25.898 60.806 15.039 1.00 52.55 ATOM 3094 N ARG 445 25.307 58.667 15.496 1.00 48.51 ATOM 3095 CA ARG 445 24.265 59.004 16.468 1.00 45.71 ATOM 3096 CB ARG 445 22.967 59.507 15.832 1.00 46.38 ATOM 3097 CG ARG 445 22.092 60.234 16.859 1.00 44.46 ATOM 3098 CD ARG 445 20.753 60.743 16.351 1.00 45.51 ATOM 3099 NE ARG 445 19.999 61.330 17.464 1.00 52.32 ATOM 3100 CZ ARG 445 18.887 62.053 17.347 1.00 53.85 ATOM 3101 NH1 ARG 445 18.294 62.533 18.437 1.00 55.79 ATOM 3102 NH2 ARG 445 18.351 62.286 16.155 1.00 58.42 ATOM 3103 C ARG 445 23.975 57.834 17.411 1.00 44.59 ATOM 3104 O ARG 445 23.439 56.801 17.012 1.00 42.64 ATOM 3105 N ASN 446 24.333 58.018 18.671 1.00 47.32 ATOM 3106 CA ASN 446 24.125 56.995 19.683 1.00 51.50 ATOM 3107 CB ASN 446 25.218 55.918 19.582 1.00 50.30 ATOM 3108 CG ASN 446 26.606 56.478 19.825 1.00 50.32 ATOM 3109 OD1 ASN 446 27.349 56.754 18.882 1.00 52.97 ATOM 3110 ND2 ASN 446 26.958 56.666 21.088 1.00 49.49 ATOM 3111 C ASN 446 24.128 57.608 21.078 1.00 52.00 ATOM 3112 O ASN 446 24.866 58.559 21.351 1.00 53.53 ATOM 3113 N ASN 447 23.336 57.015 21.967 1.00 53.99 ATOM 3114 CA ASN 447 23.195 57.460 23.358 1.00 54.97 ATOM 3115 CB ASN 447 21.887 56.927 23.940 1.00 53.00 ATOM 3116 CG ASN 447 20.722 57.051 22.976 1.00 54.20 ATOM 3117 OD1 ASN 447 20.312 58.160 22.629 1.00 59.45 ATOM 3118 ND2 ASN 447 20.189 55.916 22.530 1.00 53.02 ATOM 3119 C ASN 447 24.345 56.951 24.222 1.00 57.40 ATOM 3120 O ASN 447 24.547 57.409 25.340 1.00 62.75 ATOM 3121 N GLY 448 25.075 55.981 23.689 1.00 58.44 ATOM 3122 CA GLY 448 26.192 55.389 24.396 1.00 56.36 ATOM 3123 C GLY 448 26.432 54.065 23.700 1.00 53.77 ATOM 3124 O GLY 448 25.747 53.771 22.717 1.00 58.09 ATOM 3125 N HIS 449 27.376 53.258 24.162 1.00 49.50 ATOM 3126 CA HIS 449 27.599 52.007 23.458 1.00 48.10 ATOM 3127 CB HIS 449 29.005 51.934 22.830 1.00 55.56 ATOM 3128 CG HIS 449 29.141 52.749 21.581 1.00 61.28 ATOM 3129 CD2 HIS 449 29.963 53.783 21.278 1.00 61.16 ATOM 3130 ND1 HIS 449 28.310 52.584 20.490 1.00 63.15 ATOM 3131 CE1 HIS 449 28.613 53.486 19.576 1.00 65.47 ATOM 3132 NE2 HIS 449 29.610 54.226 20.030 1.00 65.11 ATOM 3133 C HIS 449 27.338 50.745 24.196 1.00 40.97 ATOM 3134 O HIS 449 28.120 50.321 25.031 1.00 42.17 ATOM 3135 N VAL 450 26.212 50.143 23.908 1.00 33.34 ATOM 3136 CA VAL 450 25.933 48.883 24.516 1.00 33.89 ATOM 3137 CB VAL 450 24.525 48.441 24.179 1.00 27.68 ATOM 3138 CG1 VAL 450 24.214 47.106 24.811 1.00 23.45 ATOM 3139 CG2 VAL 450 23.555 49.506 24.621 1.00 19.28 ATOM 3140 C VAL 450 26.961 48.066 23.742 1.00 42.79 ATOM 3141 O VAL 450 27.421 48.496 22.674 1.00 48.77 ATOM 3142 N SER 451 27.392 46.937 24.273 1.00 47.08 ATOM 3143 CA SER 451 28.383 46.149 23.550 1.00 46.69 ATOM 3144 CB SER 451 29.418 45.553 24.529 1.00 49.40 ATOM 3145 OG SER 451 30.187 46.575 25.155 1.00 52.97 ATOM 3146 C SER 451 27.758 45.054 22.677 1.00 44.69 ATOM 3147 O SER 451 26.524 44.869 22.643 1.00 43.38 ATOM 3148 N ALA 452 28.612 44.394 23.904 1.00 40.41 ATOM 3149 CA ALA 452 28.181 43.315 21.037 1.00 37.56 ATOM 3150 CB ALA 452 27.379 43.865 19.841 1.00 35.98 ATOM 3151 C ALA 452 29.378 42.474 20.577 1.00 35.17 ATOM 3152 O ALA 452 30.446 42.482 21.188 1.00 34.47 ATOM 3153 N GLN 453 29.215 41.832 19.438 1.00 31.36 ATOM 3154 CA GLN 453 30.208 40.947 18.882 1.00 28.35 ATOM 3155 CB GLN 453 29.638 40.360 17.578 1.00 31.30 ATOM 3156 CG GLN 453 30.246 39.018 17.163 1.00 32.89 ATOM 3157 CD GLN 453 29.737 38.530 15.832 1.00 31.23 ATOM 3158 OE1 GLN 453 30.143 39.026 14.779 1.00 34.14 ATOM 3159 NE2 GLN 453 28.845 37.556 15.868 1.00 28.65 ATOM 3160 C GLN 453 31.681 41.343 18.676 1.00 25.25 ATOM 3161 O GLN 453 32.005 42.349 18.039 1.00 25.08 ATOM 3162 N ASP 454 32.565 40.513 19.222 1.00 24.22 ATOM 3163 CA ASP 454 33.998 40.645 19.019 1.00 23.88 ATOM 3164 CB ASP 454 34.776 40.663 20.321 1.00 23.71 ATOM 3165 CG ASP 454 36.292 40.678 20.099 1.00 27.65 ATOM 3166 OD1 ASP 454 36.752 40.687 18.941 1.00 26.59 ATOM 3167 OD2 ASP 454 37.040 40.670 21.098 1.00 34.10 ATOM 3168 C ASP 454 34.274 39.332 18.299 1.00 28.07 ATOM 3169 O ASP 454 33.990 38.257 18.841 1.00 26.35 ATOM 3170 N SER 455 34.800 39.409 17.077 1.00 30.04 ATOM 3171 CA SER 455 35.073 38.204 16.273 1.00 27.99 ATOM 3172 CB SER 455 35.589 38.575 14.877 1.00 23.39 ATOM 3173 OG SER 455 36.916 39.063 14.946 1.00 32.54 ATOM 3174 C SER 455 35.966 37.112 16.882 1.00 26.74 ATOM 3175 O SER 455 35.650 35.928 16.736 1.00 28.30 ATOM 3176 N ILE 456 37.057 37.482 17.563 1.00 23.67 ATOM 3177 CA ILE 456 37.948 36.485 18.155 1.00 18.04 ATOM 3178 CB ILE 456 39.083 37.138 18.933 1.00 23.55 ATOM 3179 CG2 ILE 456 39.990 37.911 17.978 1.00 17.58 ATOM 3180 CG1 ILE 456 38.498 38.012 20.047 1.00 30.14 ATOM 3181 CD1 ILE 456 39.487 38.426 21.128 1.00 35.57 ATOM 3182 C ILE 456 37.246 35.486 19.077 1.00 20.83 ATOM 3183 O ILE 456 37.703 34.354 19.260 1.00 16.93 ATOM 3184 N ASP 457 36.138 35.896 19.673 1.00 22.41 ATOM 3185 CA ASP 457 35.416 34.996 20.550 1.00 27.43 ATOM 3186 CB ASP 457 34.324 35.751 21.328 1.00 34.30 ATOM 3187 CG ASP 457 34.900 36.788 22.308 1.00 41.24 ATOM 3188 OD1 ASP 457 34.382 37.925 22.363 1.00 44.36 ATOM 3189 OD2 ASP 457 35.874 36.471 23.032 1.00 50.52 ATOM 3190 C ASP 457 34.847 33.825 19.742 1.00 27.01 ATOM 3191 O ASP 457 34.839 32.685 20.210 1.00 31.27 ATOM 3192 N GLN 458 34.413 34.096 18.515 1.00 27.92 ATOM 3193 CA GLN 458 33.883 33.044 17.632 1.00 30.33 ATOM 3194 CB GLN 458 32.932 33.614 16.573 1.00 29.37 ATOM 3195 CG GLN 458 31.866 34.561 17.053 1.00 32.48 ATOM 3196 CD GLN 458 30.514 33.939 16.989 1.00 33.02 ATOM 3197 OE1 GLN 458 29.750 33.981 17.947 1.00 41.92 ATOM 3198 NE2 GLN 458 30.212 33.316 15.872 1.00 37.05 ATOM 3199 C GLN 458 35.037 32.357 16.869 1.00 28.95 ATOM 3200 O GLN 458 35.049 31.133 16.719 1.00 26.34 ATOM 3201 N LEU 459 35.982 33.158 16.368 1.00 24.82 ATOM 3202 CA LEU 459 37.107 32.652 15.587 1.00 19.59 ATOM 3203 CB LEU 459 37.033 33.236 14.183 1.00 17.07 ATOM 3204 CG LEU 459 35.684 32.976 13.504 1.00 19.32 ATOM 3205 CD1 LEU 459 35.541 33.890 12.331 1.00 16.44 ATOM 3206 CD2 LEU 459 35.549 31.523 13.074 1.00 11.36 ATOM 3207 C LEU 459 38.455 32.987 16.182 1.00 15.91 ATOM 3208 O LEU 459 39.175 33.815 15.651 1.00 14.53 ATOM 3209 N PRO 460 38.820 32.339 17.299 1.00 16.20 ATOM 3210 CD PRO 460 38.042 31.315 18.012 1.00 17.21 ATOM 3211 CA PRO 460 40.106 32.589 17.960 1.00 15.73 ATOM 3212 CB PRO 460 40.133 31.541 19.086 1.00 17.01 ATOM 3213 CG PRO 460 39.123 30.494 18.642 1.00 17.80 ATOM 3214 C PRO 460 41.257 32.386 17.008 1.00 16.53 ATOM 3215 O PRO 460 41.079 31.758 15.967 1.00 22.97 ATOM 3216 N PRO 461 42.426 32.982 17.302 1.00 16.43 ATOM 3217 CD PRO 461 42.687 33.873 18.451 1.00 16.11 ATOM 3218 CA PRO 461 43.615 32.858 16.455 1.00 19.04 ATOM 3219 CB PRO 461 44.550 33.938 17.011 1.00 17.90 ATOM 3220 CG PRO 461 44.190 33.962 18.467 1.00 17.10 ATOM 3221 C PRO 461 44.217 31.470 16.624 1.00 22.01 ATOM 3222 O PRO 461 43.757 30.678 17.448 1.00 25.54 ATOM 3223 N GLU 462 45.247 31.169 15.856 1.00 25.14 ATOM 3224 CA GLU 462 45.888 29.877 15.958 1.00 28.39 ATOM 3225 CB GLU 462 46.625 29.560 14.674 1.00 22.97 ATOM 3226 CG GLU 462 45.675 29.090 13.627 1.00 21.83 ATOM 3227 CD GLU 462 46.320 28.834 12.299 1.00 25.80 ATOM 3228 OE1 GLU 462 47.571 28.780 12.227 1.00 29.20 ATOM 3229 OE2 GLU 462 45.562 28.693 11.318 1.00 20.77 ATOM 3230 C GLU 462 46.780 29.678 17.181 1.00 33.43 ATOM 3231 O GLU 462 46.989 28.533 17.586 1.00 35.01 ATOM 3232 N THR 463 47.307 30.775 17.745 1.00 37.95 ATOM 3233 CA THR 463 48.170 30.767 18.946 1.00 40.65 ATOM 3234 CB THR 463 49.674 30.861 18.635 1.00 40.48 ATOM 3235 OG1 THR 463 49.945 30.372 17.321 1.00 44.41 ATOM 3236 CG2 THR 463 50.464 30.089 19.671 1.00 40.34 ATOM 3237 C THR 463 47.920 32.088 19.616 1.00 42.47 ATOM 3238 O THR 463 47.497 33.022 18.952 1.00 41.83 ATOM 3239 N THR 464 48.331 32.210 20.874 1.00 48.42 ATOM 3240 CA THR 464 48.155 33.457 21.622 1.00 55.33 ATOM 3241 CB THR 464 47.453 33.204 22.959 1.00 57.02 ATOM 3242 OG1 THR 464 48.099 32.118 23.633 1.00 62.71 ATOM 3243 CG2 THR 464 45.984 32.855 22.730 1.00 59.94 ATOM 3244 C THR 464 49.474 34.195 21.879 1.00 58.07 ATOM 3245 O THR 464 49.500 35.416 22.085 1.00 58.66 ATOM 3246 N ASP 465 50.573 33.453 21.878 1.00 61.40 ATOM 3247 CA ASP 465 51.881 34.065 22.091 1.00 65.65 ATOM 3248 CB ASP 465 52.843 33.061 22.731 1.00 66.43 ATOM 3249 CG ASP 465 52.793 31.700 22.069 1.00 64.17 ATOM 3250 OD1 ASP 465 52.245 30.777 22.709 1.00 61.40 ATOM 3251 OD2 ASP 465 53.302 31.556 20.929 1.00 62.59 ATOM 3252 C ASP 465 52.431 34.573 20.757 1.00 66.66 ATOM 3253 O ASP 465 53.641 34.569 20.518 1.00 70.16 ATOM 3254 N GLU 466 51.520 35.002 19.893 1.00 64.93 ATOM 3255 CA GLU 466 51.851 35.511 18.577 1.00 60.06 ATOM 3256 CB GLU 466 51.574 34.444 17.528 1.00 64.82 ATOM 3257 CG GLU 466 52.657 33.415 17.372 1.00 71.79 ATOM 3258 CD GLU 466 53.441 33.627 16.098 1.00 76.80 ATOM 3259 OE1 GLU 466 52.797 33.726 15.024 1.00 78.10 ATOM 3260 OE2 GLU 466 54.691 33.703 16.173 1.00 79.01 ATOM 3261 C GLU 466 50.918 36.674 18.332 1.00 56.09 ATOM 3262 O GLU 466 49.742 36.607 18.684 1.00 56.03 ATOM 3263 N PRO 467 51.447 37.799 17.831 1.00 51.07 ATOM 3264 CD PRO 467 52.847 38.171 17.597 1.00 49.21 ATOM 3265 CA PRO 467 50.566 38.933 17.572 1.00 46.48 ATOM 3266 CB PRO 467 51.486 39.931 16.858 1.00 48.89 ATOM 3267 CG PRO 467 52.701 39.128 16.465 1.00 47.91 ATOM 3268 C PRO 467 49.408 38.481 16.695 1.00 44.45 ATOM 3269 O PRO 467 49.600 37.737 15.721 1.00 42.21 ATOM 3270 N LEU 468 48.212 38.924 17.059 1.00 40.59 ATOM 3271 CA LEU 468 46.995 38.561 16.352 1.00 40.01 ATOM 3272 CB LEU 468 45.839 39.431 16.837 1.00 41.89 ATOM 3273 CG LEU 468 44.463 39.052 16.305 1.00 41.02 ATOM 3274 CD1 LEU 468 44.105 37.664 16.775 1.00 42.02 ATOM 3275 CD2 LEU 468 43.447 40.052 16.786 1.00 44.91 ATOM 3276 C LEU 468 47.086 38.602 14.824 1.00 37.52 ATOM 3277 O LEU 468 46.714 37.647 14.153 1.00 36.89 ATOM 3278 N GLU 469 47.622 39.690 14.286 1.00 38.63 ATOM 3279 CA GLU 469 47.761 39.881 12.831 1.00 36.54 ATOM 3280 CB GLU 469 48.312 41.280 12.543 1.00 36.96 ATOM 3281 CG GLU 469 49.822 41.402 12.774 1.00 36.18 ATOM 3282 CD GLU 469 50.168 42.065 14.072 1.00 33.77 ATOM 3283 OE1 GLU 469 51.233 42.715 14.107 1.00 36.01 ATOM 3284 OE2 GLU 469 49.382 41.945 15.043 1.00 30.63 AT6M 3285 C GLU 469 48.682 38.859 12.174 1.00 35.12 ATOM 3286 O GLU 469 48.816 38.801 10.941 1.00 32.72 ATOM 3287 N LYS 470 49.357 38.106 13.033 1.00 37.81 ATOM 3288 CA LYS 470 50.305 37.094 12.640 1.00 36.11 ATOM 3289 CB LYS 470 51.646 37.391 13.271 1.00 40.29 ATOM 3290 CG LYS 470 52.622 37.924 12.260 1.00 50.88 ATOM 3291 CD LYS 470 53.757 36.936 12.100 1.00 59.58 ATOM 3292 CE LYS 470 53.236 35.529 11.834 1.00 61.72 ATOM 3293 NZ LYS 470 53.976 34.506 12.630 1.00 64.89 ATOM 3294 C LYS 470 49.865 35.711 13.034 1.00 36.21 ATOM 3295 O LYS 470 50.504 34.733 12.659 1.00 39.63 ATOM 3296 N ALA 471 48.771 35.613 13.779 1.00 33.18 ATOM 3297 CA ALA 471 48.284 34.310 14.182 1.00 29.06 ATOM 3298 CB ALA 471 48.598 34.060 15.651 1.00 25.21 ATOM 3299 C ALA 471 46.799 34.083 13.911 1.00 29.06 ATOM 3300 O ALA 471 46.295 33.013 14.238 1.00 31.11 ATOM 3301 N TYR 472 46.091 35.046 13.311 1.00 26.54 ATOM 3302 CA TYR 472 44.650 34.861 13.057 1.00 23.18 ATOM 3303 CB TYR 472 43.999 36.124 12.507 1.00 18.72 ATOM 3304 CG TYR 472 44.489 36.511 11.157 1.00 22.75 ATOM 3305 CD1 TYR 472 43.860 36.031 10.020 1.00 25.95 ATOM 3306 CE1 TYR 472 44.294 36.381 8.756 1.00 27.97 ATOM 3307 CD2 TYR 472 45.575 37.365 11.003 1.00 22.21 ATOM 3308 CE2 TYR 472 46.022 37.738 9.739 1.00 26.59 ATOM 3309 CZ TYR 472 45.372 37.233 8.609 1.00 32.17 ATOM 3310 OH TYR 472 45.797 37.549 7.327 1.00 36.52 ATOM 3311 C TYR 472 44.325 33.647 12.183 1.00 20.40 ATOM 3312 O TYR 472 45.114 33.226 11.354 1.00 22.10 ATOM 3313 N SER 473 43.161 33.073 12.393 1.00 15.42 ATOM 3314 CA SER 473 42.773 31.901 11.654 1.00 18.76 ATOM 3315 CB SER 473 42.068 30.968 12.596 1.00 20.56 ATOM 3316 OG SER 473 40.944 31.663 13.113 1.00 18.80 ATOM 3317 C SER 473 41.843 32.190 10.482 1.00 21.56 ATOM 3318 O SER 473 41.654 31.317 9.623 1.00 22.66 ATOM 3319 N HIS 474 41.203 33.366 10.478 1.00 21.81 ATOM 3320 CA HIS 474 40.269 33.739 9.405 1.00 19.11 ATOM 3321 CB HIS 474 38.841 33.314 9.752 1.00 15.89 ATOM 3322 CG HIS 474 38.702 31.860 10.093 1.00 12.80 ATOM 3323 CD2 HIS 474 39.069 31.170 11.192 1.00 8.32 ATOM 3324 ND1 HIS 474 38.030 30.966 9.289 1.00 17.15 ATOM 3325 CE1 HIS 474 37.981 29.793 9.880 1.00 13.99 ATOM 3326 NE2 HIS 474 38.605 29.889 11.040 1.00 16.43 ATOM 3327 C HIS 474 40.234 35.218 9.045 1.00 20.13 ATOM 3328 O HIS 474 40.591 36.079 9.837 1.00 22.30 ATOM 3329 N GLN 475 39.750 35.493 7.844 1.00 22.49 ATOM 3330 CA GLN 475 39.613 36.848 7.328 1.00 23.06 ATOM 3331 CB GLN 475 40.571 37.061 6.155 1.00 27.55 ATOM 3332 CG GLN 475 40.762 35.814 5.317 1.00 44.65 ATOM 3333 CD GLN 475 41.572 36.048 4.068 1.00 53.46 ATOM 3334 OE1 GLN 475 42.346 35.175 3.640 1.00 61.88 ATOM 3335 NE2 GLN 475 41.399 37.226 3.458 1.00 53.85 ATOM 3336 C GLN 475 38.161 37.067 6.880 1.00 20.99 ATOM 3337 O GLN 475 37.449 36.108 6.561 1.00 19.73 ATOM 3338 N LEU 476 37.700 38.314 6.965 1.00 23.59 ATOM 3339 CA LEU 476 36.337 38.691 6.566 1.00 23.47 ATOM 3340 CB LEU 476 36.004 40.117 7.035 1.00 18.61 ATOM 3341 CG LEU 476 34.553 40.579 6.997 1.00 13.45 ATOM 3342 CD1 LEU 476 33.742 39.763 7.990 1.00 17.94 ATOM 3343 CD2 LEU 476 34.476 42.042 7.354 1.00 16.38 ATOM 3344 C LEU 476 36.224 38.573 5.037 1.00 25.91 ATOM 3345 O LEU 476 37.137 38.974 4.278 1.00 24.64 ATOM 3346 N ASN 477 35.111 37.999 4.601 1.00 23.61 ATOM 3347 CA ASN 477 34.851 37.764 3.200 1.00 25.65 ATOM 3348 CB ASN 477 34.815 36.245 2.978 1.00 26.73 ATOM 3349 CG ASN 477 34.376 35.858 1.594 1.00 30.01 ATOM 3350 OD1 ASN 477 33.219 35.499 1.369 1.00 34.38 ATOM 3351 ND2 ASN 477 35.299 35.899 0.659 1.00 27.30 ATOM 3352 C ASN 477 33.560 38.435 2.701 1.00 27.24 ATOM 3353 O ASN 477 33.509 38.929 1.575 1.00 30.67 ATOM 3354 N TYR 478 32.583 38.597 3.587 1.00 28.03 ATOM 3355 CA TYR 478 31.283 39.159 3.214 1.00 26.02 ATOM 3356 CB TYR 478 30.437 38.021 2.617 1.00 28.82 ATOM 3357 CG TYR 478 29.454 38.399 1.528 1.00 29.16 ATOM 3358 CD1 TYR 478 29.910 38.749 0.244 1.00 29.31 ATOM 3359 CE1 TYR 478 29.019 39.022 -0.799 1.00 29.21 ATOM 3360 CD2 TYR 478 28.072 38.337 1.746 1.00 25.53 ATOM 3361 CE2 TYR 478 27.170 38.609 0.702 1.00 31.35 ATOM 3362 CZ TYR 478 27.663 38.949 -0.565 1.00 28.53 ATOM 3363 OH TYR 478 26.818 39.188 -1.609 1.00 29.12 ATOM 3364 C TYR 478 30.536 39.751 4.435 1.00 27.26 ATOM 3365 O TYR 478 30.816 39.412 5.582 1.00 26.91 ATOM 3366 N ALA 479 29.592 40.642 4.163 1.00 26.82 ATOM 3367 CA ALA 479 28.761 41.273 5.178 1.00 26.75 ATOM 3368 CB ALA 479 29.283 42.665 5.500 1.00 26.06 ATOM 3369 C ALA 479 27.377 41.336 4.519 1.00 25.07 ATOM 3370 O ALA 479 27.265 41.549 3.309 1.00 28.22 ATOM 3371 N GLU 480 26.329 41.078 5.275 1.00 24.88 ATOM 3372 CA GLU 480 25.008 41.108 4.677 1.00 30.15 ATOM 3373 CB GLU 480 24.750 39.764 4.005 1.00 30.81 ATOM 3374 CG GLU 480 23.335 39.525 3.511 1.00 34.30 ATOM 3375 CD GLU 480 23.158 38.143 2.856 1.00 37.80 ATOM 3376 OE1 GLU 480 22.025 37.848 2.398 1.00 38.54 ATOM 3377 OE2 GLU 480 24.138 37.352 2.802 1.00 38.29 ATOM 3378 C GLU 480 23.955 41.400 5.725 1.00 31.66 ATOM 3379 O GLU 480 23.977 40.780 6.787 1.00 34.86 ATOM 3380 N CYS 481 23.077 42.373 5.453 1.00 32.22 ATOM 3381 CA CYS 481 22.013 42.740 6.391 1.00 31.34 ATOM 3382 CB CYS 481 21.725 44.221 6.334 1.00 27.71 ATOM 3383 SG CYS 481 23.102 45.167 6.880 1.00 33.86 ATOM 3384 C CYS 481 20.719 42.008 6.158 1.00 33.16 ATOM 3385 O CYS 481 20.363 41.713 5.027 1.00 36.23 ATOM 3386 N PHE 482 20.033 41.691 7.247 1.00 34.11 ATOM 3387 CA PHE 482 18.753 41.009 7.206 1.00 30.22 ATOM 3388 CB PHE 482 18.845 39.637 7.849 1.00 34.49 ATOM 3389 CG PHE 482 19.608 38.641 7.023 1.00 40.80 ATOM 3390 CD1 PHE 482 20.998 38.659 6.989 1.00 42.96 ATOM 3391 CD2 PHE 482 18.937 37.683 6.265 1.00 46.84 ATOM 3392 CE1 PHE 482 21.717 37.738 6.212 1.00 44.53 ATOM 3393 CE2 PHE 482 19.646 36.751 5.478 1.00 47.79 ATOM 3394 CZ PHE 482 21.040 36.783 5.456 1.00 46.14 ATOM 3395 C PHE 482 17.850 41.918 7.987 1.00 30.71 ATOM 3396 O PHE 482 18.312 42.716 8.798 1.00 33.95 ATOM 3397 N LEU 483 16.561 41.811 7.758 1.00 27.58 ATOM 3398 CA LEU 483 15.647 42.703 8.420 1.00 27.73 ATOM 3399 CB LEU 483 14.738 43.377 7.394 1.00 24.99 ATOM 3400 CG LEU 483 15.270 44.192 6.226 1.00 21.74 ATOM 3401 CD1 LEU 483 14.098 44.627 5.397 1.00 25.27 ATOM 3402 CD2 LEU 483 16.019 45.395 6.678 1.00 21.38 ATOM 3403 C LEU 483 14.778 41.959 9.401 1.00 31.66 ATOM 3404 O LEU 483 14.371 40.810 9.164 1.00 31.14 ATOM 3405 N MET 484 14.447 42.645 10.481 1.00 33.44 ATOM 3406 CA MET 484 13.585 42.068 11.479 1.00 36.28 ATOM 3407 CB MET 484 13.973 42.576 12.866 1.00 36.13 ATOM 3408 CG MET 484 15.308 42.089 13.352 1.00 38.45 ATOM 3409 SD MET 484 15.491 42.483 15.082 1.00 45.99 ATOM 3410 CE MET 484 16.389 43.963 15.012 1.00 41.27 ATOM 3411 C MET 484 12.132 42.427 11.152 1.00 38.11 ATOM 3412 O MET 484 11.852 43.387 10.416 1.00 41.32 ATOM 3413 N GLN 485 11.219 41.624 11.680 1.00 42.45 ATOM 3414 CA GLN 485 9.782 41.819 11.511 1.00 46.46 ATOM 3415 CB GLN 485 9.037 40.519 11.822 1.00 47.26 ATOM 3416 CG GLN 485 9.396 39.376 10.884 1.00 48.83 ATOM 3417 CD GLN 485 8.697 38.093 11.257 1.00 51.68 ATOM 3418 OE1 GLN 485 9.325 37.185 11.774 1.00 56.20 ATOM 3419 NE2 GLN 485 7.386 38.015 11.014 1.00 54.56 ATOM 3420 C GLN 485 9.303 42.928 12.446 1.00 46.51 ATOM 3421 O GLN 485 10.050 43.400 13.307 1.00 43.94 ATOM 3422 N ASP 486 8.054 43.344 12.278 1.00 48.98 ATOM 3423 CA ASP 486 7.502 44.417 13.099 1.00 51.60 ATOM 3424 CB ASP 486 7.163 43.889 14.498 1.00 55.79 ATOM 3425 CG ASP 486 6.188 44.788 15.242 1.00 60.84 ATOM 3426 OD1 ASP 486 5.712 45.784 14.657 1.00 66.91 ATOM 3427 OD2 ASP 486 5.899 44.500 16.424 1.00 65.08 ATOM 3428 C ASP 486 8.507 45.588 13.163 1.00 50.17 ATOM 3429 O ASP 486 8.714 46.203 14.213 1.00 51.11 ATOM 3430 N ARG 487 9.168 45.826 12.030 1.00 49.23 ATOM 3431 CA ARG 487 10.150 46.895 11.851 1.00 50.67 ATOM 3432 CB ARG 487 9.443 48.192 11.482 1.00 59.54 ATOM 3433 CG ARG 487 8.846 48.250 10.104 1.00 69.48 ATOM 3434 CD ARG 487 7.999 49.490 10.008 1.00 77.95 ATOM 3435 NE ARG 487 7.637 49.805 8.634 1.00 90.05 ATOM 3436 CZ ARG 487 7.217 51.006 8.243 1.00 96.14 ATOM 3437 NH1 ARG 487 6.905 51.221 6.961 1.00 99.29 ATOM 3438 NH2 ARG 487 7.108 51.995 9.138 1.00 97.66 ATOM 3439 C ARG 487 11.067 47.204 13.017 1.00 48.25 ATOM 3440 O ARG 487 11.190 48.369 13.405 1.00 50.28 ATOM 3441 N ARG 488 11.721 46.198 13.580 1.00 43.30 ATOM 3442 CA ARG 488 12.622 46.470 14.693 1.00 44.26 ATOM 3443 CB ARG 488 12.667 45.285 15.667 1.00 45.30 ATOM 3444 CG ARG 488 11.324 44.941 16.242 1.00 38.80 ATOM 3445 CD ARG 488 10.692 46.175 16.832 1.00 34.28 ATOM 3446 NE ARG 488 9.310 45.889 17.157 1.00 33.22 ATOM 3447 CZ ARG 488 8.922 45.236 18.248 1.00 34.98 ATOM 3448 NH1 ARG 488 9.815 44.815 19.131 1.00 34.60 ATOM 3449 NH2 ARG 488 7.641 44.928 18.422 1.00 38.53 ATOM 3450 C ARG 488 14.037 46.883 14.252 1.00 44.49 ATOM 3451 O ARG 488 14.851 47.349 15.075 1.00 44.38 ATOM 3452 N GLY 489 14.323 46.738 12.958 1.00 40.82 ATOM 3453 CA GLY 489 15.634 47.110 12.461 1.00 38.10 ATOM 3454 C GLY 489 16.300 46.037 11.622 1.00 37.57 ATOM 3455 O GLY 489 15.618 45.144 11.094 1.00 36.28 ATOM 3456 N THR 490 17.628 46.125 11.493 1.00 35.19 ATOM 3457 CA THR 490 18.379 45.152 10.711 1.00 30.90 ATOM 3458 CB THR 490 18.837 45.747 9.348 1.00 29.73 ATOM 3459 OG1 THR 490 20.169 46.257 9.440 1.00 33.88 ATOM 3460 CG2 THR 490 17.924 46.870 8.941 1.00 24.06 ATOM 3461 C THR 490 19.566 44.566 11.478 1.00 31.16 ATOM 3462 O THR 490 20.287 45.296 12.156 1.00 31.36 ATOM 3463 N ILE 491 19.705 43.235 11.423 1.00 28.86 ATOM 3464 CA ILE 491 20.802 42.496 12.073 1.00 26.73 ATOM 3465 CB ILE 491 20.320 41.170 12.803 1.00 26.17 ATOM 3466 CG2 ILE 491 20.602 41.207 14.292 1.00 29.86 ATOM 3467 CG1 ILE 491 18.854 40.882 12.535 1.00 27.37 ATOM 3468 CD1 ILE 491 18.659 39.784 11.547 1.00 32.39 ATOM 3469 C ILE 491 21.786 42.045 10.992 1.00 24.72 ATOM 3470 O ILE 491 21.402 41.341 10.055 1.00 27.21 ATOM 3471 N PRO 492 23.041 42.490 11.061 1.00 23.25 ATOM 3472 CD PRO 492 23.497 43.732 11.703 1.00 20.04 ATOM 3473 CA PRO 492 24.005 42.064 10.036 1.00 24.76 ATOM 3474 CB PRO 492 25.050 43.171 10.010 1.00 23.01 ATOM 3475 CG PRO 492 24.301 44.338 10.611 1.00 24.54 ATOM 3476 C PRO 492 24.634 40.677 10.326 1.00 27.40 ATOM 3477 O PRO 492 24.626 40.210 11.476 1.00 27.66 ATOM 3478 N PHE 493 25.124 40.027 9.263 1.00 30.29 ATOM 3479 CA PHE 493 25.775 38.701 9.293 1.00 30.16 ATOM 3480 CB PHE 493 25.033 37.677 8.406 1.00 36.53 ATOM 3481 CG PHE 493 23.702 37.212 8.925 1.00 45.55 ATOM 3482 CD1 PHE 493 22.830 38.075 9.597 1.00 52.04 ATOM 3483 CD2 PHE 493 23.279 35.916 8.660 1.00 47.34 ATOM 3484 CE1 PHE 493 21.540 37.651 9.992 1.00 52.95 ATOM 3485 CE2 PHE 493 22.007 35.486 9.044 1.00 51.52 ATOM 3486 CZ PHE 493 21.131 36.354 9.713 1.00 52.07 ATOM 3487 C PHE 493 27.141 38.832 8.601 1.00 28.46 ATOM 3488 O PHE 493 27.207 39.375 7.490 1.00 27.20 ATOM 3489 N PHE 494 28.194 38.268 9.193 1.00 22.47 ATOM 3490 CA PHE 494 29.525 38.266 8.576 1.00 21.79 ATOM 3491 CB PHE 494 30.585 38.704 9.569 1.00 24.52 ATOM 3492 CG PHE 494 30.596 40.163 9.819 1.00 31.15 ATOM 3493 CD1 PHE 494 30.974 40.662 11.056 1.00 28.30 ATOM 3494 CD2 PHE 494 30.267 41.059 8.793 1.00 33.44 ATOM 3495 CE1 PHE 494 31.028 42.043 11.265 1.00 31.41 ATOM 3496 CE2 PHE 494 30.315 42.445 8.992 1.00 29.26 ATOM 3497 CZ PHE 494 30.700 42.935 10.227 1.00 25.91 ATOM 3498 C PHE 494 29.882 36.851 8.065 1.00 24.01 ATOM 3499 O PHE 494 29.352 35.851 8.568 1.00 20.12 ATOM 3500 N THR 495 30.753 36.786 7.057 1.00 20.49 ATOM 3501 CA THR 495 31.220 35.533 6.467 1.00 18.98 ATOM 3502 CB THR 495 30.712 35.369 5.053 1.00 22.01 ATOM 3503 OG1 THR 495 29.297 35.571 5.035 1.00 19.23 ATOM 3504 CG2 THR 495 31.056 33.962 4.531 1.00 19.98 ATOM 3505 C THR 495 32.745 35.571 6.397 1.00 19.99 ATOM 3506 O THR 495 33.314 36.519 5.857 1.00 17.46 ATOM 3507 N TRP 496 33.403 34.527 6.893 1.00 19.16 ATOM 3508 CA TRP 496 34.858 34.492 6.921 1.00 19.00 ATOM 3509 CB TRP 496 35.328 34.416 8.378 1.00 19.02 ATOM 3510 CG TRP 496 34.732 35.457 9.277 1.00 17.89 ATOM 3511 CD2 TRP 496 35.405 36.601 9.851 1.00 20.54 ATOM 3512 CE2 TRP 496 34.438 37.342 10.579 1.00 20.61 ATOM 3513 CE3 TRP 496 36.730 37.071 9.825 1.00 19.34 ATOM 3514 CD1 TRP 496 33.424 35.543 9.681 1.00 19.86 ATOM 3515 NE1 TRP 496 33.241 36.680 10.458 1.00 23.72 ATOM 3516 CZ2 TRP 496 34.756 38.525 11.263 1.00 18.67 ATOM 3517 CZ3 TRP 496 37.044 38.263 10.521 1.00 15.75 ATOM 3518 CH2 TRP 496 36.059 38.963 11.223 1.00 12.02 ATOM 3519 C TRP 496 35.465 33.318 6.147 1.00 18.54 ATOM 3520 O TRP 496 34.789 32.321 5.914 1.00 16.59 ATOM 3521 N THR 497 36.729 33.459 5.735 1.00 17.86 ATOM 3522 CA THR 497 37.463 32.391 5.040 1.00 20.19 ATOM 3523 CB THR 497 37.694 32.650 3.524 1.00 19.90 ATOM 3524 OG1 THR 497 38.546 33.787 3.320 1.00 19.60 ATOM 3525 CG2 THR 497 36.390 32.884 2.835 1.00 18.46 ATOM 3526 C THR 497 38.811 32.171 5.773 1.00 23.90 ATOM 3527 O THR 497 39.338 33.085 6.443 1.00 24.61 ATOM 3528 N HIS 498 39.328 30.947 5.681 1.00 20.24 ATOM 3529 CA HIS 498 40.544 30.546 6.355 1.00 18.34 ATOM 3530 CB HIS 498 40.721 29.034 6.233 1.00 17.33 ATOM 3531 CG HIS 498 41.575 28.440 7.312 1.00 19.72 ATOM 3532 CD2 HIS 498 41.296 28.147 8.603 1.00 17.68 ATOM 3533 ND1 HIS 498 42.889 28.069 7.112 1.00 18.83 ATOM 3534 CE1 HIS 498 43.385 27.578 8.233 1.00 18.42 ATOM 3535 NE2 HIS 498 42.438 27.615 9.154 1.00 20.50 ATOM 3536 C HIS 498 41.795 31.233 5.871 1.00 19.67 ATOM 3537 O HIS 498 42.023 31.388 4.674 1.00 22.08 ATOM 3538 N ARG 499 42.679 31.520 6.809 1.00 21.68 ATOM 3539 CA ARG 499 43.937 32.177 6.475 1.00 24.21 ATOM 3540 CB ARG 499 44.705 32.506 7.753 1.00 27.17 ATOM 3541 CG ARG 499 45.003 31.299 8.637 1.00 33.94 ATOM 3542 CD ARG 499 46.383 30.756 8.400 1.00 38.30 ATOM 3543 NE ARG 499 46.458 29.344 8.771 1.00 51.54 ATOM 3544 CZ ARG 499 47.386 28.500 8.324 1.00 55.23 ATOM 3545 NH1 ARG 499 47.369 27.229 8.722 1.00 57.57 ATOM 3546 NH2 ARG 499 48.322 28.920 7.473 1.00 55.32 ATOM 3547 C ARG 499 44.813 31.328 5.556 1.00 23.51 ATOM 3548 O ARG 499 45.787 31.816 4.999 1.00 27.69 ATOM 3549 N SER 500 44.476 30.060 5.390 1.00 19.69 ATOM 3550 CA SER 500 45.300 29.227 4.561 1.00 21.75 ATOM 3551 CB SER 500 45.031 27.736 4.818 1.00 21.16 ATOM 3552 OG SER 500 43.708 27.365 4.461 1.00 15.96 ATOM 3553 C SER 500 45.178 29.533 3.082 1.00 25.26 ATOM 3554 O SER 500 46.068 29.152 2.323 1.00 31.57 ATOM 3555 N VAL 501 44.089 30.184 2.656 1.00 24.13 ATOM 3556 CA VAL 501 43.888 30.486 1.226 1.00 21.77 ATOM 3557 CB VAL 501 42.554 31.137 0.974 1.00 18.09 ATOM 3558 CG1 VAL 501 42.479 31.606 -0.440 1.00 15.04 ATOM 3559 CG2 VAL 501 41.437 30.158 1.276 1.00 18.35 ATOM 3560 C VAL 501 44.976 31.359 0.599 1.00 25.52 ATOM 3561 O VAL 501 45.155 32.518 0.963 1.00 31.84 ATOM 3562 N ASP 502 45.666 30.800 -0.385 1.00 26.11 ATOM 3563 CA ASP 502 46.751 31.478 -1.073 1.00 25.59 ATOM 3564 CB ASP 502 47.673 30.432 -1.694 1.00 25.96 ATOM 3565 CG ASP 502 48.924 31.022 -2.302 1.00 29.25 ATOM 3566 OD1 ASP 502 49.141 32.243 -2.177 1.00 32.80 ATOM 3567 OD2 ASP 502 49.702 30.241 -2.904 1.00 28.44 ATOM 3568 C ASP 502 46.153 32.319 -2.170 1.00 27.90 ATOM 3569 O ASP 502 45.642 31.780 -3.153 1.00 29.56 ATOM 3570 N PHE 503 46.230 33.635 -2.030 1.00 29.10 ATOM 3571 CA PHE 503 45.691 34.514 -3.059 1.00 29.42 ATOM 3572 CB PHE 503 45.842 35.970 -2.639 1.00 31.35 ATOM 3573 CG PHE 503 45.414 36.927 -3.690 1.00 32.60 ATOM 3574 CD1 PHE 503 44.084 37.022 -4.043 1.00 31.44 ATOM 3575 CD2 PHE 503 46.351 37.691 -4.368 1.00 35.02 ATOM 3576 CE1 PHE 503 43.682 37.862 -5.059 1.00 34.84 ATOM 3577 CE2 PHE 503 45.965 38.535 -5.383 1.00 35.77 ATOM 3578 CZ PHE 503 44.623 38.623 -5.733 1.00 35.90 ATOM 3579 C PHE 503 46.367 34.296 -4.430 1.00 30.03 ATOM 3580 O PHE 503 45.708 34.347 -5.480 1.00 30.07 ATOM 3581 N PHE 504 47.667 34.001 -4.401 1.00 25.40 ATOM 3582 CA PHE 504 48.459 33.792 -5.606 1.00 20.19 ATOM 3583 CB PHE 504 49.896 34.175 -5.308 1.00 21.87 ATOM 3584 CG PHE 504 50.033 35.605 -4.960 1.00 26.09 ATOM 3585 CD1 PHE 504 50.089 36.004 -3.635 1.00 23.60 ATOM 3586 CD2 PHE 504 49.954 36.579 -5.963 1.00 25.37 ATOM 3587 CE1 PHE 504 50.051 37.354 -3.310 1.00 26.79 ATOM 3588 CE2 PHE 504 49.914 37.927 -5.653 1.00 27.28 ATOM 3589 CZ PHE 504 49.959 38.321 -4.323 1.00 26.34 ATOM 3590 C PHE 504 48.421 32.462 -6.321 1.00 20.08 ATOM 3591 O PHE 504 49.106 32.285 -7.328 1.00 19.90 ATOM 3592 N ASN 505 47.650 31.518 -5.809 1.00 19.82 ATOM 3593 CA ASN 505 47.581 30.208 -6.433 1.00 19.32 ATOM 3594 CB ASN 505 46.744 30.294 -7.702 1.00 24.30 ATOM 3595 CG ASN 505 45.284 30.542 -7.415 1.00 25.23 ATOM 3596 OD1 ASN 505 44.874 30.529 -6.261 1.00 31.04 ATOM 3597 ND2 ASN 505 44.488 30.756 -8.461 1.00 26.30 ATOM 3598 C ASN 505 48.983 29.683 -6.756 1.00 20.70 ATOM 3599 O ASN 505 49.216 29.101 -7.817 1.00 20.32 ATOM 3600 N THR 506 49.917 29.914 -5.842 1.00 16.35 ATOM 3601 CA THR 506 51.305 29.505 -6.010 1.00 20.86 ATOM 3602 CB THR 506 52.150 30.067 -4.801 1.00 24.90 ATOM 3603 OG1 THR 506 51.926 31.483 -4.667 1.00 30.23 ATOM 3604 CG2 THR 506 53.640 29.820 -4.972 1.00 22.07 ATOM 3605 C THR 506 51.514 27.973 -6.141 1.00 23.99 ATOM 3606 O THR 506 50.883 27.197 -5.423 1.00 27.58 ATOM 3607 N ILE 507 52.354 27.542 -7.086 1.00 22.61 ATOM 3608 CA ILE 507 52.684 26.128 -7.255 1.00 18.50 ATOM 3609 CB ILE 507 52.811 25.719 -8.720 1.00 17.29 ATOM 3610 CG2 ILE 507 53.059 24.277 -8.808 1.00 15.63 ATOM 3611 CG1 ILE 507 51.570 26.091 -9.523 1.00 20.82 ATOM 3612 CD1 ILE 507 50.307 25.413 -9.066 1.00 29.01 ATOM 3613 C ILE 507 54.082 26.024 -6.663 1.00 22.48 ATOM 3614 O ILE 507 55.009 26.678 -7.147 1.00 24.75 ATOM 3615 N ASP 508 54.220 25.237 -5.598 1.00 28.69 ATOM 3616 CA ASP 508 55.490 25.018 -4.872 1.00 29.24 ATOM 3617 CB ASP 508 55.196 24.244 -3.576 1.00 30.26 ATOM 3618 CG ASP 508 56.258 24.441 -2.513 1.00 30.30 ATOM 3619 OD1 ASP 508 56.151 25.441 -1.789 1.00 40.59 ATOM 3620 OD2 ASP 508 57.179 23.608 -2.368 1.00 33.88 ATOM 3621 C ASP 508 56.497 24.218 -5.700 1.00 28.60 ATOM 3622 O ASP 508 56.116 23.312 -6.426 1.00 31.91 ATOM 3623 N ALA 509 57.785 24.472 -5.518 1.00 28.24 ATOM 3624 CA ALA 509 58.805 23.760 -6.296 1.00 29.33 ATOM 3625 CB ALA 509 60.049 24.613 -6.412 1.00 35.65 ATOM 3626 C ALA 509 59.201 22.391 -5.788 1.00 27.56 ATOM 3627 O ALA 509 59.779 21.599 -6.547 1.00 25.79 ATOM 3628 N GLU 510 58.963 22.166 -4.491 1.00 27.06 ATOM 3629 CA GLU 510 59.303 20.920 -3.783 1.00 29.89 ATOM 3630 CB GLU 510 60.020 21.242 -2.458 1.00 38.97 ATOM 3631 CG GLU 510 61.233 22.188 -2.502 1.00 49.84 ATOM 3632 CD GLU 510 62.515 21.514 -2.997 1.00 58.12 ATOM 3633 OE1 GLU 510 63.358 22.221 -3.599 1.00 60.55 ATOM 3634 OE2 GLU 510 62.691 20.286 -2.779 1.00 63.36 ATOM 3635 C GLU 510 58.076 20.055 -3.435 1.00 29.54 ATOM 3636 O GLU 510 58.046 18.858 -3.696 1.00 30.98 ATOM 3637 N LYS 511 57.101 20.655 -2.764 1.00 22.60 ATOM 3638 CA LYS 511 55.905 19.944 -2.366 1.00 22.05 ATOM 3639 CB LYS 511 55.161 20.748 -1.307 1.00 26.10 ATOM 3640 CG LYS 511 55.963 21.228 -0.151 1.00 26.97 ATOM 3641 CD LYS 511 55.046 21.938 0.826 1.00 27.62 ATOM 3642 CE LYS 511 55.824 22.589 1.947 1.00 27.53 ATOM 3643 NZ LYS 511 56.428 23.877 1.516 1.00 38.15 ATOM 3644 C LYS 511 54.900 19.680 -3.493 1.00 20.67 ATOM 3645 O LYS 511 54.972 20.269 -4.573 1.00 17.60 ATOM 3646 N ILE 512 53.932 18.819 -3.180 1.00 19.36 ATOM 3647 CA ILE 512 52.829 18.484 -4.068 1.00 20.42 ATOM 3648 CB ILE 512 52.170 17.166 -3.668 1.00 16.67 ATOM 3649 CG2 ILE 512 50.863 16.971 -4.416 1.00 9.97 ATOM 3650 CG1 ILE 512 53.148 16.022 -3.921 1.00 12.77 ATOM 3651 CD1 ILE 512 52.728 14.748 -3.293 1.00 12.13 ATOM 3652 C ILE 512 51.860 19.607 -3.748 1.00 25.62 ATOM 3653 O ILE 512 51.643 19.919 -2.569 1.00 26.02 ATOM 3654 N THR 513 51.299 20.224 -4.781 1.00 23.63 ATOM 3655 CA THR 513 50.398 21.344 -4.594 1.00 21.04 ATOM 3656 CB THR 513 50.929 22.537 -5.378 1.00 21.80 ATOM 3657 OG1 THR 513 52.250 22.847 -4.910 1.00 19.60 ATOM 3658 CG2 THR 513 50.041 23.733 -5.217 1.00 16.11 ATOM 3659 C THR 513 48.980 21.046 -5.013 1.00 21.44 ATOM 3660 O THR 513 48.760 20.534 -6.089 1.00 22.73 ATOM 3661 N GLN 514 48.024 21.302 -4.125 1.00 24.53 ATOM 3662 CA GLN 514 46.605 21.088 -4.432 1.00 24.32 ATOM 3663 CB GLN 514 45.826 20.522 -3.230 1.00 19.75 ATOM 3664 CG GLN 514 46.008 19.039 -2.972 1.00 16.42 ATOM 3665 CD GLN 514 44.859 18.416 -2.171 1.00 17.95 ATOM 3666 OE1 GLN 514 44.379 17.318 -2.501 1.00 13.78 ATOM 3667 NE2 GLN 514 44.395 19.121 -1.141 1.00 10.87 ATOM 3668 C GLN 514 46.004 22.441 -4.799 1.00 22.49 ATOM 3669 O GLN 514 46.181 23.397 -4.047 1.00 25.77 ATOM 3670 N LEU 515 45.357 22.522 -5.970 1.00 20.22 ATOM 3671 CA LEU 515 44.694 23.734 -6.442 1.00 19.38 ATOM 3672 CB LEU 515 45.116 24.108 -7.883 1.00 24.66 ATOM 3673 CG LEU 515 44.498 25.381 -8.514 1.00 19.43 ATOM 3674 CD1 LEU 515 44.854 26.618 -7.735 1.00 17.74 ATOM 3675 CD2 LEU 515 44.941 25.544 -9.931 1.00 20.58 ATOM 3676 C LEU 515 43.197 23.474 -6.393 1.00 21.82 ATOM 3677 O LEU 515 42.670 22.664 -7.172 1.00 20.91 ATOM 3678 N PRO 516 42.509 24.057 -5.391 1.00 23.18 ATOM 3679 CD PRO 516 43.000 24.926 -4.299 1.00 20.43 ATOM 3680 CA PRO 516 41.062 23.849 -5.293 1.00 20.71 ATOM 3681 CB PRO 516 40.677 24.713 -4.086 1.00 22.88 ATOM 3682 CG PRO 516 41.941 24.755 -3.249 1.00 18.38 ATOM 3683 C PRO 516 40.457 24.382 -6.600 1.00 21.60 ATOM 3684 O PRO 516 40.820 25.459 -7.105 1.00 20.78 ATOM 3685 N VAL 517 39.550 23.624 -7.174 1.00 19.37 ATOM 3686 CA VAL 517 38.964 24.045 -8.431 1.00 19.42 ATOM 3687 CB VAL 517 38.135 22.859 -9.010 1.00 17.07 ATOM 3688 CG1 VAL 517 36.717 22.848 -8.468 1.00 18.76 ATOM 3689 CG2 VAL 517 38.203 22.842 -10.505 1.00 19.36 ATOM 3690 C VAL 511 38.206 25.410 -8.324 1.00 20.59 ATOM 3691 O VAL 517 38.076 26.146 -9.307 1.00 16.82 ATOM 3692 N VAL 518 37.813 25.785 -7.10b 1.00 23.40 ATOM 3693 CA VAL 518 37.115 27.053 -6.842 1.00 19.17 ATOM 3694 CB VAL 518 36.353 27.093 -5.486 1.00 10.97 ATOM 3695 CG1 VAL 518 35.202 26.153 -5.513 1.00 7.06 ATOM 3696 CG2 VAL 518 37.302 26.810 -4.333 1.00 9.27 ATOM 3697 C VAL 518 38.049 28.258 -6.877 1.00 21.48 ATOM 3698 O VAL 518 37.595 29.399 -6.689 1.00 23.23 ATOM 3699 N LYS 519 39.342 28.022 -7.089 1.00 18.73 ATOM 3700 CA LYS 519 40.297 29.124 -7.173 1.00 19.19 ATOM 3701 CB LYS 519 41.681 28.685 -6.676 1.00 21.90 ATOM 3702 CG LYS 519 41.673 28.268 -5.224 1.00 21.02 ATOM 3703 CD LYS 519 41.574 29.452 -4.322 1.00 12.82 ATOM 3704 CE LYS 519 42.966 29.886 -4.023 1.00 12.46 ATOM 3705 NZ LYS 519 42.930 31.325 -4.032 1.00 21.04 ATOM 3706 C LYS 519 40.376 29.653 -8.608 1.00 19.96 ATOM 3707 O LYS 519 41.147 30.566 -8.897 1.00 23.17 ATOM 3708 N ALA 520 39.642 29.016 -9.517 1.00 21.32 ATOM 3709 CA ALA 520 39.572 29.439 -10.916 1.00 24.50 ATOM 3710 CB ALA 520 38.624 28.531 -11.700 1.00 18.52 ATOM 3711 C ALA 520 39.008 30.844 -10.906 1.00 28.46 ATOM 3712 O ALA 520 38.227 31.196 -10.012 1.00 31.25 ATOM 3713 N TYR 521 39.373 31.649 -11.893 1.00 31.66 ATOM 3714 CA TYR 521 38.844 32.996 -11.943 1.00 30.02 ATOM 3715 CB TYR 521 39.943 33.981 -12.295 1.00 33.11 ATOM 3716 CG TYR 521 40.519 33.781 -13.660 1.00 39.15 ATOM 3717 CD1 TYR 521 39.878 34.304 -14.777 1.00 39.69 ATOM 3718 CE1 TYR 521 40.423 34.180 -16.043 1.00 44.05 ATOM 3719 CD2 TYR 521 41.733 33.115 -13.840 1.00 44.01 ATOM 3720 CE2 TYR 521 42.299 32.982 -15.116 1.00 44.87 ATOM 3721 CZ TYR 521 41.635 33.527 -16.213 1.00 44.96 ATOM 3722 OH TYR 521 42.177 33.480 -17.480 1.00 46.99 ATOM 3723 C TYR 521 37.663 33.115 -12.897 1.00 29.31 ATOM 3724 O TYR 521 36.953 34.115 -12.892 1.00 30.01 ATOM 3725 N ALA 522 37.405 32.058 -13.654 1.00 27.46 ATOM 3726 CA ALA 522 36.321 32.062 -14.626 1.00 25.98 ATOM 3727 CB ALA 522 36.836 32.608 -15.952 1.00 25.45 ATOM 3728 C ALA 522 35.783 30.654 -14.814 1.00 24.28 ATOM 3729 O ALA 522 36.520 29.701 -14.620 1.00 28.55 ATOM 3730 N LEU 523 34.501 30.524 -15.152 1.00 22.39 ATOM 3731 CA LEU 523 33.873 29.215 -15.368 1.00 25.19 ATOM 3732 CB LEU 523 32.917 28.831 -14.244 1.00 22.10 ATOM 3733 CG LEU 523 33.289 28.143 -12.941 1.00 21.99 ATOM 3734 CD1 LEU 523 31.973 27.665 -12.307 1.00 17.94 ATOM 3735 CD2 LEU 523 34.212 26.962 -13.171 1.00 21.88 ATOM 3736 C LEU 523 33.028 29.278 -16.617 1.00 29.42 ATOM 3737 O LEU 523 32.535 30.348 -16.958 1.00 34.90 ATOM 3738 N SER 524 32.802 28.133 -17.258 1.00 30.06 ATOM 3739 CA SER 524 31.998 28.085 -18.463 1.00 31.24 ATOM 3740 CB SER 524 32.529 27.015 -19.437 1.00 30.18 ATOM 3741 OG SER 524 31.702 25.859 -19.512 1.00 33.88 ATOM 3742 C SER 524 30.558 27.827 -18.055 1.00 34.56 ATOM 3743 O SER 524 30.298 27.349 -16.955 1.00 35.42 ATOM 3744 N SER 525 29.630 28.145 -18.953 1.00 40.50 ATOM 3745 CA SER 525 28.186 27.978 -18.745 1.00 41.55 ATOM 3746 CB SER 525 27.443 28.284 -20.053 1.00 44.75 ATOM 3747 OG SER 525 28.180 29.192 -20.862 1.00 50.22 ATOM 3748 C SER 525 27.793 26.570 -18.310 1.00 41.55 ATOM 3749 O SER 525 26.793 26.386 -17.615 1.00 41.77 ATOM 3750 N GLY 526 28.565 25.579 -18.748 1.00 41.99 ATOM 3751 CA GLY 526 28.251 24.200 -18.427 1.00 42.33 ATOM 3752 C GLY 526 28.766 23.641 -17.118 1.00 39.74 ATOM 3753 O GLY 526 28.651 22.443 -16.887 1.00 41.33 ATOM 3754 N ALA 527 29.321 24.483 -16.262 1.00 35.00 ATOM 3755 CA ALA 527 29.840 24.010 -15.005 1.00 31.00 ATOM 3756 CB ALA 527 31.339 24.130 -15.004 1.00 25.11 ATOM 3757 C ALA 527 29.241 24.865 -13.917 1.00 32.01 ATOM 3758 O ALA 527 28.887 26.013 -14.153 1.00 35.83 ATOM 3759 N SER 528 29.079 24.303 -12.732 1.00 31.08 ATOM 3760 CA SER 528 28.546 25.076 -11.624 1.00 31.31 ATOM 3761 CB SER 528 27.040 24.870 -11.516 1.00 30.58 ATOM 3762 OG SER 528 26.734 23.533 -11.161 1.00 36.73 ATOM 3763 C SER 528 29.232 24.686 -10.315 1.00 29.29 ATOM 3764 O SER 528 29.679 23.545 -10.159 1.00 26.49 ATOM 3765 N ILE 529 29.409 25.659 -9.424 1.00 27.83 ATOM 3766 CA ILE 529 30.005 25.375 -8.130 1.00 27.64 ATOM 3767 CB ILE 529 30.721 26.596 -7.498 1.00 27.04 ATOM 3768 CG2 ILE 529 31.322 26.216 -6.134 1.00 18.53 ATOM 3769 CG1 ILE 529 31.846 27.094 -8.415 1.00 19.40 ATOM 3770 CD1 ILE 529 32.895 26.065 -8.767 1.00 21.82 ATOM 3771 C ILE 529 28.834 24.871 -7.275 1.00 30.57 ATOM 3772 O ILE 529 27.726 25.411 -7.288 1.00 32.70 ATOM 3773 N ILE 530 29.084 23.801 -6.556 1.00 31.83 ATOM 3774 CA ILE 530 28.059 23.163 -5.786 1.00 31.82 ATOM 3775 CB ILE 530 27.571 21.955 -6.653 1.00 32.98 ATOM 3776 CG2 ILE 530 27.538 20.628 -5.926 1.00 32.68 ATOM 3777 CG1 ILE 530 26.272 22.355 -7.338 1.00 39.74 ATOM 3778 CD1 ILE 530 25.682 21.281 -8.215 1.00 51.04 ATOM 3779 C ILE 530 28.594 22.862 -4.382 1.00 33.34 ATOM 3780 O ILE 530 29.791 23.012 -4.129 1.00 34.98 ATOM 3781 N GLU 531 27.705 22.578 -3.441 1.00 31.94 ATOM 3782 CA GLU 531 28.123 22.303 -2.083 1.00 34.44 ATOM 3783 CB GLU 531 26.929 22.278 -1.159 1.00 45.98 ATOM 3784 CG GLU 531 26.914 23.434 -0.196 1.00 66.36 ATOM 3785 CD GLU 531 26.232 23.083 1.115 1.00 77.90 ATOM 3786 OE1 GLU 531 24.979 22.972 1.130 1.00 81.37 ATOM 3787 OE2 GLU 531 26.962 22.911 2.124 1.00 82.42 ATOM 3788 C GLU 531 28.895 21.012 -1.933 1.00 32.72 ATOM 3789 O GLU 531 28.470 19.961 -2.401 1.00 29.66 ATOM 3790 N GLY 532 30.021 21.093 -1.232 1.00 30.18 ATOM 3791 CA GLY 532 30.846 19.927 -1.030 1.00 27.98 ATOM 3792 C GLY 532 30.138 18.922 -0.153 1.00 29.77 ATOM 3793 O GLY 532 29.254 19.277 0.632 1.00 29.92 ATOM 3794 N PRO 533 30.529 17.651 -0.251 1.00 28.01 ATOM 3795 CD PRO 533 31.657 17.234 -1.095 1.00 26.16 ATOM 3796 CA PRO 533 29.991 16.517 0.499 1.00 28.35 ATOM 3797 CB PRO 533 30.744 15.341 -0.105 1.00 30.57 ATOM 3798 CG PRO 533 32.064 15.941 -0.451 1.00 31.83 ATOM 3799 C PRO 533 30.261 16.645 2.000 1.00 28.68 ATOM 3800 O PRO 533 29.501 16.132 2.846 1.00 30.87 ATOM 3801 N GLY 534 31.365 17.301 2.333 1.00 26.38 ATOM 3802 CA GLY 534 31.669 17.488 3.734 1.00 22.29 ATOM 3803 C GLY 534 33.105 17.254 4.099 1.00 22.73 ATOM 3804 O GLY 534 33.609 17.901 5.014 1.00 24.94 ATOM 3805 N PHE 535 33.772 16.350 3.386 1.00 20.12 ATOM 3806 CA PHE 535 35.165 16.021 3.690 1.00 18.54 ATOM 3807 CB PHE 535 35.314 14.500 3.811 1.00 15.96 ATOM 3808 CG PHE 535 34.747 13.766 2.642 1.00 18.55 ATOM 3809 CD1 PHE 535 35.480 13.633 1.461 1.00 17.25 ATOM 3810 CD2 PHE 535 33.434 13.320 2.667 1.00 15.57 ATOM 3811 CE1 PHE 535 34.904 13.080 0.323 1.00 16.51 ATOM 3812 CE2 PHE 535 32.853 12.764 1.528 1.00 17.82 ATOM 3813 CZ PHE 535 33.588 12.647 0.357 1.00 13.09 ATOM 3814 C PHE 535 36.195 16.550 2.686 1.00 18.37 ATOM 3815 O PHE 535 37.365 16.192 2.771 1.00 18.67 ATOM 3816 N THR 536 35.797 17.366 1.717 1.00 17.09 ATOM 3817 CA THR 536 36.803 17.850 0.793 1.00 20.39 ATOM 3818 CB THR 536 36.269 17.966 -0.610 1.00 19.96 ATOM 3819 OG1 THR 536 35.193 18.909 -0.632 1.00 17.87 ATOM 3820 CG2 THR 536 35.820 16.617 -1.094 1.00 19.15 ATOM 3821 C THR 536 37.412 19.165 1.262 1.00 23.00 ATOM 3822 O THR 536 37.941 19.960 0.491 1.00 24.82 ATOM 3823 N GLY 537 37.357 19.402 2.551 1.00 27.76 ATOM 3824 CA GLY 537 37.947 20.616 3.033 1.00 33.89 ATOM 3825 C GLY 537 37.002 21.709 2.752 1.00 33.32 ATOM 3826 O GLY 537 35.911 21.463 2.287 1.00 38.06 ATOM 3827 N GLY 538 37.449 22.924 2.980 1.00 37.93 ATOM 3828 CA GLY 538 36.582 24.038 2.771 1.00 42.84 ATOM 3829 C GLY 538 35.777 23.873 1.519 1.00 47.29 ATOM 3830 O GLY 538 34.558 24.065 1.468 1.00 54.74 ATOM 3831 N ASP 539 36.477 23.366 0.535 1.00 45.55 ATOM 3832 CA ASP 539 35.907 23.168 -0.756 1.00 41.92 ATOM 3833 CB ASP 539 36.785 22.204 -1.574 1.00 45.21 ATOM 3834 CG ASP 539 37.857 22.920 -2.353 1.00 49.53 ATOM 3835 OD1 ASP 539 38.701 23.577 -1.693 1.00 44.03 ATOM 3836 OD2 ASP 539 37.835 22.831 -3.616 1.00 51.70 ATOM 3837 C ASP 539 34.450 22.797 -0.928 1.00 34.91 ATOM 3838 O ASP 539 33.806 22.129 -0.116 1.00 26.81 ATOM 3839 N LEU 540 33.969 23.372 -2.011 1.00 29.82 ATOM 3840 CA LEU 540 32.688 23.155 -2.588 1.00 27.20 ATOM 3841 CB LEU 540 32.005 24.485 -2.857 1.00 24.69 ATOM 3842 CG LEU 540 31.540 25.134 -1.561 1.00 20.73 ATOM 3843 CD1 LEU 540 30.836 26.432 -1.858 1.00 25.75 ATOM 3844 CD2 LEU 540 30.620 24.208 -0.826 1.00 15.49 ATOM 3845 C LEU 540 33.270 22.506 -3.863 1.00 25.13 ATOM 3846 O LEU 540 34.456 22.645 -4.147 1.00 22.50 ATOM 3847 N LEU 541 32.488 21.736 -4.587 1.00 26.66 ATOM 3848 CA LEU 541 33.029 21.059 -5.759 1.00 29.40 ATOM 3849 CB LEU 541 32.562 19.590 -5.753 1.00 24.79 ATOM 3850 CG LEU 541 32.965 18.655 -4.619 1.00 19.38 ATOM 3851 CD1 LEU 541 32.132 17.434 -4.653 1.00 23.37 ATOM 3852 CD2 LEU 541 34.394 18.273 -4.756 1.00 26.40 ATOM 3853 C LEU 541 32.437 21.707 -6.967 1.00 31.74 ATOM 3854 O LEU 541 31.630 22.614 -6.830 1.00 35.14 ATOM 3855 N PHE 542 32.874 21.319 -8.156 1.00 33.03 ATOM 3856 CA PHE 542 32.165 21.827 -9.305 1.00 34.85 ATOM 3857 CB PHE 542 32.946 22.894 -10.101 1.00 41.04 ATOM 3858 CG PHE 542 33.556 22.451 -11.401 1.00 41.46 ATOM 3859 CD1 PHE 542 34.706 23.080 -11.832 1.00 43.22 ATOM 3860 CD2 PHE 542 33.007 21.453 -12.192 1.00 43.55 ATOM 3861 CE1 PHE 542 35.299 22.725 -13.010 1.00 50.04 ATOM 3862 CE2 PHE 542 33.583 21.080 -13.372 1.00 51.19 ATOM 3863 CZ PHE 542 34.740 21.715 -13.791 1.00 54.39 ATOM 3864 C PHE 542 31.563 20.654 -10.066 1.00 35.15 ATOM 3865 O PHE 542 32.207 19.597 -10.215 1.00 34.08 ATOM 3866 N LEU 543 30.273 20.786 -10.371 1.00 32.50 ATOM 3867 CA LEU 543 29.531 19.770 -11.111 1.00 31.66 ATOM 3868 CB LEU 543 28.057 19.692 -10.650 1.00 29.24 ATOM 3869 CG LEU 543 27.107 18.714 -11.379 1.00 31.50 ATOM 3870 CD1 LEU 543 27.411 17.275 -11.030 1.00 30.64 ATOM 3871 CD2 LEU 543 25.663 19.008 -11.049 1.00 31.69 ATOM 3872 C LEU 543 29.610 20.159 -12.587 1.00 29.13 ATOM 3873 O LEU 543 29.603 21.340 -12.933 1.00 23.01 ATOM 3874 N LYS 544 29.727 19.165 -13.455 1.00 32.67 ATOM 3875 CA LYS 544 29.813 19.442 -14.876 1.00 36.80 ATOM 3876 CB LYS 544 31.056 18.803 -15.476 1.00 37.11 ATOM 3877 CG LYS 544 31.272 19.198 -16.904 1.00 37.33 ATOM 3878 CD LYS 544 32.647 18.823 -17.345 1.00 42.84 ATOM 3879 CE LYS 544 33.093 17.482 -16.791 1.00 40.97 ATOM 3880 NZ LYS 544 33.958 17.669 -15.599 1.00 48.30 ATOM 3881 C LYS 544 28.579 18.979 -15.606 1.00 36.90 ATOM 3882 O LYS 544 28.158 17.827 -15.449 1.00 32.22 ATOM 3883 N GLU 545 27.993 19.919 -16.352 1.00 40.87 ATOM 3884 CA GLU 545 26.786 19.708 -17.158 1.00 49.67 ATOM 3885 CB GLU 545 25.803 20.872 -16.986 1.00 57.26 ATOM 3886 CG GLU 545 26.062 21.808 -15.801 1.00 70.57 ATOM 3887 CD GLU 545 25.347 21.393 -14.524 1.00 79.49 ATOM 3888 OE1 GLU 545 24.824 20.253 -14.461 1.00 82.86 ATOM 3889 OE2 GLU 545 25.300 22.223 -13.581 1.00 84.89 ATOM 3890 C GLU 545 27.132 19.591 -18.652 1.00 49.21 ATOM 3891 O GLU 545 26.745 18.634 -19.318 1.00 47.69 ATOM 3892 N SER 546 27.831 20.593 -19.176 1.00 52.91 ATOM 3893 CA SER 546 28.236 20.626 -20.585 1.00 56.07 ATOM 3894 CB SER 546 27.641 21.863 -21.289 1.00 59.19 ATOM 3895 OG SER 546 26.228 21.789 -21.462 1.00 58.56 ATOM 3896 C SER 546 29.760 20.718 -20.596 1.00 55.58 ATOM 3897 O SER 546 30.338 21.272 -19.659 1.00 56.91 ATOM 3898 N SER 547 30.397 20.214 -21.654 1.00 54.06 ATOM 3899 CA SER 547 31.859 20.228 -21.759 1.00 54.75 ATOM 3900 CB SER 547 32.336 18.833 -22.125 1.00 55.22 ATOM 3901 6G SER 547 31.784 17.902 -21.213 1.00 58.09 ATOM 3902 C SER 547 32.417 21.251 -22.753 1.00 53.95 ATOM 3903 O SER 547 31.722 21.596 -23.705 1.00 58.59 ATOM 3904 N ASN 548 33.662 21.716 -22.544 1.00 52.76 ATOM 3905 CA ASN 548 34.306 22.712 -23.428 1.00 51.19 ATOM 3906 CB ASN 548 33.366 23.914 -23.633 1.00 56.75 ATOM 3907 CG ASN 548 32.797 24.464 -22.328 1.00 58.52 ATOM 3908 OD1 ASN 548 33.076 23.955 -21.249 1.00 58.90 ATOM 3909 ND2 ASN 548 32.001 25.517 -22.431 1.00 67.62 ATOM 3910 C ASN 548 35.720 23.222 -23.044 1.00 48.17 ATOM 3911 O ASN 548 36.727 22.791 -23.663 1.00 46.64 ATOM 3912 N SER 549 35.751 24.252 -22.199 1.00 47.03 ATOM 3913 CA SER 549 36.959 24.892 -21.650 1.00 38.92 ATOM 3914 CB SER 549 37.491 25.999 -22.547 1.00 42.82 ATOM 3915 OG SER 549 37.544 27.249 -21.877 1.00 43.37 ATOM 3916 C SER 549 36.313 25.450 -20.394 1.00 34.96 ATOM 3917 O SER 549 35.966 26.625 -20.271 1.00 31.37 ATOM 3918 N ILE 550 36.020 24.485 -19.541 1.00 32.88 ATOM 3919 CA ILE 550 35.342 24.657 -18.291 1.00 32.30 ATOM 3920 CB ILE 550 35.247 23.317 -17.576 1.00 31.25 ATOM 3921 CG2 ILE 550 34.300 23.433 -16.429 1.00 34.89 ATOM 3922 CG1 ILE 550 34.674 22.283 -18.542 1.00 30.40 ATOM 3923 CD1 ILE 550 34.896 20.896 -18.129 1.00 36.71 ATOM 3924 C ILE 550 35.865 25.727 -17.364 1.00 31.36 ATOM 3925 O ILE 550 35.151 26.673 -17.068 1.00 36.41 ATOM 3926 N ALA 551 37.109 25.629 -16.932 1.00 28.45 ATOM 3927 CA ALA 551 37.595 26.631 -16.020 1.00 23.43 ATOM 3928 CB ALA 551 37.505 26.093 -14.589 1.00 21.57 ATOM 3929 C ALA 551 38.994 27.128 -16.350 1.00 22.09 ATOM 3930 O ALA 551 39.793 26.406 -16.951 1.00 20.34 ATOM 3931 N LYS 552 39.260 28.387 -16.008 1.00 21.43 ATOM 3932 CA LYS 552 40.561 28.996 -16.251 1.00 23.88 ATOM 3933 CB LYS 552 40.452 30.215 -17.161 1.00 23.98 ATOM 3934 CG LYS 552 39.861 29.894 -18.522 1.00 32.51 ATOM 3935 CD LYS 552 39.797 31.113 -19.444 1.00 37.66 ATOM 3936 CE LYS 552 38.344 31.508 -19.707 1.00 46.35 ATOM 3937 Z LYS 552 37.473 30.364 -20.166 1.00 51.47 ATOM 3938 C LYS 552 41.122 29.414 -14.924 1.00 24.89 ATOM 3939 O LYS 552 40.390 29.870 -14.049 1.00 25.99 ATOM 3940 N PHE 553 42.435 29.291 -14.790 1.00 27.07 ATOM 3941 CA PHE 553 43.116 29.623 -13.555 1.00 26.79 ATOM 3942 CB PHE 553 43.630 28.346 -12.810 1.00 28.52 ATOM 3943 CG PHE 553 42.560 27.342 -12.397 1.00 24.78 ATOM 3944 CD1 PHE 553 42.189 26.305 -13.251 1.00 25.89 ATOM 3945 CD2 PHE 553 41.967 27.407 -11.135 1.00 25.91 ATOM 3946 CE1 PHE 553 41.238 25.352 -12.853 1.00 29.14 ATOM 3947 CE2 PHE 553 41.021 26.461 -10.726 1.00 25.20 ATOM 3948 CZ PHE 553 40.652 25.433 -11.584 1.00 24.73 ATOM 3949 C PHE 553 44.366 30.352 -13.957 1.00 25.61 ATOM 3950 O PHE 553 44.850 30.198 -15.065 1.00 25.20 ATOM 3951 N LYS 554 44.874 31.171 -13.062 1.00 25.03 ATOM 3952 CA LYS 554 46.157 31.764 -13.296 1.00 27.95 ATOM 3953 CB LYS 554 46.126 33.275 -13.408 1.00 30.03 ATOM 3954 CG LYS 554 47.524 33.810 -13.114 1.00 39.43 ATOM 3955 CD LYS 554 47.787 35.200 -13.624 1.00 50.21 ATOM 3956 CE LYS 554 49.197 35.626 -13.209 1.00 54.07 ATOM 3957 NZ LYS 554 49.529 36.998 -13.675 1.00 56.26 ATOM 3958 C LYS 554 46.907 31.312 -12.029 1.00 28.45 ATOM 3959 O LYS 554 46.364 31.376 -10.913 1.00 28.90 ATOM 3960 N VAL 555 48.106 30.771 -12.205 1.00 26.35 ATOM 3961 CA VAL 555 48.886 30.278 -11.082 1.00 23.89 ATOM 3962 CB VAL 555 49.143 28.753 -11.215 1.00 23.89 ATdM 3963 CG1 VAL 555 47.848 27.965 -11.005 1.00 19.80 ATOM 3964 CG2 VAL 555 49.693 28.436 -12.580 1.00 24.10 ATOM 3965 C VAL 555 50.203 31.036 -10.957 1.00 26.91 ATOM 3966 O VAL 555 50.634 31.705 -11.892 1.00 29.30 ATOM 3967 N THR 556 50.819 30.966 -9.785 1.00 27.03 ATOM 3968 CA THR 556 52.077 31.644 -9.544 1.00 23.49 ATOM 3969 CB THR 556 51.953 32.599 -8.367 1.00 23.49 ATOM 3970 OG1 THR 556 51.091 33.676 -8.743 1.00 24.29 ATOM 3971 CG2 THR 556 53.315 33.174 -7.982 1.00 22.99 ATOM 3972 C THR 556 53.234 30.690 -9.289 1.00 26.69 ATOM 3973 O THR 556 53.159 29.815 -8.420 1.00 27.95 ATOM 3974 N LEU 557 54.317 30.872 -10.035 1.00 27.71 ATOM 3975 CA LEU 557 55.500 30.038 -9.877 1.00 30.22 ATOM 3976 CB LEU 557 55.827 29.295 -11.180 1.00 21.61 ATOM 3977 CG LEU 557 54.939 28.087 -11.479 1.00 15.95 ATOM 3978 CD1 LEU 557 53.843 28.430 -12.423 1.00 12.75 ATOM 3979 CD2 LEU 557 55.766 26.986 -12.049 1.00 14.32 ATOM 3980 C LEU 557 56.644 30.948 -9.506 1.00 36.22 ATOM 3981 O LEU 557 56.571 32.146 -9.733 1.00 42.68 ATOM 3982 N ASN 558 57.646 30.402 -8.834 1.00 42.11 ATOM 3983 CA ASN 558 58.828 31.174 -8.458 1.00 43.14 ATOM 3984 CB ASN 558 59.146 31.050 -6.950 1.00 47.42 ATOM 3985 CG ASN 558 59.198 29.602 -6.457 1.00 51.14 ATOM 3986 OD1 ASN 558 60.280 29.070 -6.176 1.00 45.86 ATOM 3987 ND2 ASN 558 58.022 28.969 -6.316 1.00 53.80 ATOM 3988 C ASN 558 59.952 30.628 -9.328 1.00 44.63 ATOM 3989 O ASN 558 59.741 29.657 -10.066 1.00 46.90 ATOM 3990 N SER 559 61.128 31.247 -9.270 1.00 43.06 ATOM 3991 CA SER 559 62.270 30.812 -10.079 1.00 43.61 ATOM 3992 CB SER 559 63.496 31.652 -9.741 1.00 44.38 ATOM 3993 OG SER 559 63.328 32.976 -10.226 1.00 50.82 ATOM 3994 C SER 559 62.598 29.315 -9.984 1.00 41.12 ATOM 3995 O SER 559 62.856 28.652 -10.995 1.00 41.23 ATOM 3996 N ALA 560 62.598 28.786 -8.768 1.00 39.09 ATOM 3997 CA ALA 560 62.868 27.378 -8.580 1.00 34.53 ATOM 3998 CB ALA 560 63.016 27.069 -7.113 1.00 37.40 ATOM 3999 C ALA 560 61.719 26.583 -9.189 1.00 33.31 ATOM 4000 O ALA 560 61.945 25.591 -9.869 1.00 35.43 ATOM 4001 N ALA 561 60.489 27.052 -8.999 1.00 31.76 ATOM 4002 CA ALA 561 59.330 26.347 -9.544 1.00 29.93 ATOM 4003 CB ALA 561 58.064 26.850 -8.906 1.00 28.61 ATOM 4004 C ALA 561 59.249 26.449 -11.066 1.00 30.20 ATOM 4005 O ALA 561 58.607 25.630 -11.713 1.00 31.33 ATOM 4006 N LEU 562 59.922 27.442 -11.638 1.00 32.60 ATOM 4007 CA LEU 562 59.933 27.635 -13.088 1.00 34.08 ATOM 4008 CB LEU 562 60.209 29.106 -13.438 1.00 33.88 ATOM 4009 CG LEU 562 59.000 30.047 -13.329 1.00 34.94 ATOM 4010 CD1 LEU 562 59.424 31.495 -13.482 1.00 35.38 ATOM 4011 CD2 LEU 562 57.953 29.681 -14.373 1.00 32.01 ATOM 4612 C LEU 562 60.899 26.703 -13.835 1.00 34.58 ATOM 4013 O LEU 562 60.647 26.331 -14.979 1.00 33.64 ATOM 4014 N LEU 563 61.992 26.314 -13.182 1.00 37.75 ATOM 4015 CA LEU 563 62.990 25.406 -13.773 1.00 40.21 ATOM 4016 CB LEU 563 64.290 25.475 -12.963 1.00 41.41 ATOM 4017 CG LEU 563 65.333 26.561 -13.202 1.00 42.05 ATOM 4018 CD1 LEU 563 66.149 26.819 -11.939 1.00 43.00 ATOM 4019 CD2 LEU 563 66.231 26.107 -14.322 1.00 44.06 ATOM 4020 C LEU 563 62.492 23.961 -13.691 1.00 41.90 ATOM 4021 O LEU 563 63.112 23.034 -14.212 1.00 45.81 ATOM 4022 N GLN 564 61.357 23.789 -13.036 1.00 41.36 ATOM 4023 CA GLN 564 60.777 22.487 -12.774 1.00 39.60 ATOM 4024 CB GLN 564 60.189 22.569 -11.349 1.00 43.83 ATOM 4025 CG GLN 564 60.106 21.286 -10.543 1.00 50.18 ATOM 4026 CD GLN 564 61.469 20.739 -10.147 1.00 53.72 ATOM 4027 OE1 GLN 564 62.310 21.439 -9.558 1.00 55.36 ATOM 4028 NE2 GLN 564 61.690 19.470 -10.460 1.00 59.83 ATOM 4029 C GLN 564 59.683 22.074 -13.761 1.00 35.38 ATOM 4030 O GLN 564 59.102 22.912 -14.449 1.00 36.05 ATOM 4031 N ARG 565 59.416 20.771 -13.818 1.00 33.68 ATOM 4032 CA ARG 565 58.333 20.220 -14.637 1.00 34.60 ATOM 4033 CB ARG 565 58.830 19.257 -15.726 1.00 38.02 ATOM 4034 CG ARG 565 59.353 19.990 -16.363 1.00 40.53 ATOM 4035 CD ARG 565 59.021 19.276 -18.259 1.00 38.89 ATOM 4036 NE ARG 565 58.289 20.150 -19.172 1.00 40.20 ATOM 4037 CZ ARG 565 57.235 19.770 -19.887 1.00 42.15 ATOM 4038 NH1 ARG 565 56.630 20.637 -20.684 1.00 42.80 ATOM 4039 NH2 ARG 565 56.793 18.519 -19.821 1.00 45.49 ATOM 4040 C ARG 565 57.386 19.528 -13.658 1.00 29.39 ATOM 4041 O ARG 565 57.806 19.117 -12.573 1.00 26.69 ATOM 4042 N TYR 566 56.131 19.368 -14.052 1.00 27.44 ATOM 4043 CA TYR 566 55.125 18.807 -13.162 1.00 24.88 ATOM 4044 CB TYR 566 54.241 19.954 -12.630 1.00 24.68 ATOM 4045 CG TYR 566 55.022 21.022 -11.889 1.00 24.57 ATOM 4046 CD1 TYR 566 55.656 22.065 -12.580 1.00 23.18 ATOM 4047 CE1 TYR 566 56.479 22.981 -11.908 1.00 22.35 ATOM 4048 CD2 TYR 566 55.218 20.933 -10.504 1.00 21.68 ATOM 4049 CE2 TYR 566 56.027 21.835 -9.833 1.00 23.53 ATOM 4050 CZ TYR 566 56.657 22.845 -10.539 1.00 19.14 ATOM 4051 OH TYR 566 57.511 23.668 -9.870 1.00 29.33 ATOM 4052 C TYR 566 54.215 17.762 -13.760 1.00 26.96 ATOM 4053 O TYR 566 53.827 17.845 -14.923 1.00 26.47 ATOM 4054 N ARG 567 53.861 16.785 -12.937 1.00 28.74 ATOM 4055 CA ARG 567 52.938 15.725 -13.318 1.00 27.05 ATOM 4056 CB ARG 567 53.342 14.413 -12.647 1.00 25.39 ATOM 4057 CG ARG 567 52.790 13.157 -13.294 1.00 33.50 ATOM 4058 CD ARG 567 53.135 11.892 -12.489 1.00 35.21 ATOM 4059 NE ARG 567 52.052 11.476 -11.599 1.00 37.84 ATOM 4060 CZ ARG 567 52.230 10.952 -10.389 1.00 37.80 ATOM 4061 NH1 ARG 567 51.186 10.619 -9.660 1.00 36.93 ATOM 4062 NH2 ARG 567 53.443 10.783 -9.891 1.00 42.04 ATOM 4063 C ARG 567 51.645 16.261 -12.689 1.00 29.34 ATOM 4064 O ARG 567 51.678 16.847 -11.607 1.00 28.88 ATOM 4065 N VAL 568 50.537 16.155 -13.406 1.00 29.48 ATOM 4066 CA VAL 568 49.240 16.616 -12.929 1.00 23.50 ATOM 4067 CB VAL 568 48.517 17.435 -14.054 1.00 29.72 ATOM 4068 CG1 VAL 568 47.083 17.817 -13.659 1.00 25.49 ATOM 4069 CG2 VAL 568 49.309 18.685 -14.382 1.00 28.25 ATOM 4070 C VAL 568 48.390 15.395 -12.545 1.00 23.91 ATOM 4071 O VAL 568 48.400 14.367 -13.236 1.00 26.41 ATOM 4072 N ARG 569 47.707 15.500 -11.411 1.00 22.32 ATOM 4073 CA ARG 569 46.798 14.475 -10.887 1.00 21.06 ATOM 4074 CB ARG 569 47.270 14.042 -9.543 1.00 19.44 ATOM 4075 CG ARG 569 47.930 12.741 -9.372 1.00 20.01 ATOM 4076 CD ARG 569 47.969 12.675 -7.867 1.00 16.43 ATOM 4077 NE ARG 569 48.963 11.790 -7.329 1.00 17.92 ATOM 4078 CZ ARG 569 49.377 11.807 -6.069 1.00 12.56 ATOM 4079 NH1 ARG 569 50.295 10.928 -5.686 1.00 8.11 ATOM 4080 NH2 ARG 569 48.885 12.683 -5.215 1.00 7.02 ATOM 4081 C ARG 569 45.492 15.220 -10.600 1.00 22.50 ATOM 4082 O ARG 569 45.535 16.336 -10.105 1.00 25.09 ATOM 4083 N ILE 570 44.343 14.598 -10.799 1.00 21.96 ATOM 4084 CA ILE 570 43.072 15.268 -10.535 1.00 21.79 ATOM 4085 CB ILE 570 42.279 15.497 -11.871 1.00 24.30 ATOM 4086 CG2 ILE 570 40.750 15.555 -11.652 1.00 21.29 ATOM 4087 CG1 ILE 570 42.745 16.804 -12.494 1.00 21.98 ATOM 4088 CD1 ILE 570 43.373 16.637 -13.802 1.00 22.97 ATOM 4089 C ILE 570 42.240 14.451 -9.563 1.00 19.98 ATOM 4090 O ILE 570 42.061 13.258 -9.775 1.00 22.62 ATOM 4091 N ARG 571 41.764 15.073 -8.484 1.00 22.31 ATOM 4092 CA ARG 571 40.927 14.380 -7.502 1.00 19.02 ATOM 4093 CB ARG 571 41.173 14.917 -6.091 1.00 20.56 ATOM 4094 CG ARG 571 40.276 14.283 -5.015 1.00 30.48 ATOM 4095 CD ARG 571 41.093 13.628 -3.905 1.00 37.09 ATOM 4096 NE ARG 571 40.302 13.065 -2.802 1.00 44.17 ATOM 4097 CZ ARG 571 39.627 13.786 -1.896 1.00 49.87 ATOM 4098 NH1 ARG 571 39.607 15.129 -1.950 1.00 44.30 ATOM 4099 NH2 ARG 571 39.057 13.163 -0.861 1.00 47.17 ATOM 4100 C ARG 571 39.505 14.657 -7.982 1.00 18.92 ATOM 4101 O ARG 571 39.075 15.825 -8.064 1.00 15.94 ATOM 4102 N TYR 572 38.784 13.588 -8.316 1.00 16.89 ATOM 4103 CA TYR 572 37.441 13.715 -8.860 1.00 14.77 ATOM 4104 CB TYR 572 37.537 13.636 -10.385 1.00 16.10 ATOM 4105 CG TYR 572 37.920 12.249 -10.863 1.00 19.08 ATOM 4106 CD1 TYR 572 36.942 11.366 -11.339 1.00 19.90 ATOM 4107 CE1 TYR 572 37.245 10.048 -11.669 1.00 16.28 ATOM 4108 CD2 TYR 572 39.237 11.778 -10.742 1.00 20.80 ATOM 4109 CE2 TYR 572 39.561 10.445 -11.070 1.00 22.00 ATOM 4110 CZ TYR 572 38.551 9.582 -11.525 1.00 21.96 ATOM 4111 OH TYR 572 38.799 8.241 -11.769 1.00 17.33 ATOM 4112 C TYR 572 36.551 12.579 -8.398 1.00 16.70 ATOM 4113 O TYR 572 36.994 11.674 -7.706 1.00 17.05 ATOM 4114 N ALA 573 35.298 12.634 -8.830 1.00 17.73 ATOM 4115 CA ALA 573 34.280 11.618 -8.558 1.00 18.71 ATOM 4116 CB ALA 573 33.439 12.013 -7.357 1.00 15.72 ATOM 4117 C ALA 573 33.440 11.645 -9.845 1.00 19.61 ATOM 4118 O ALA 573 33.025 12.709 -10.291 1.00 21.78 ATOM 4119 N SER 574 33.174 10.496 -10.444 1.00 20.78 ATOM 4120 CA SER 574 32.442 10.490 -11.702 1.00 18.28 ATOM 4121 CB SER 574 33.441 10.726 -12.839 1.00 20.54 ATOM 4122 OG SER 574 32.924 10.279 -14.066 1.00 18.88 ATOM 4123 C SER 574 31.695 9.201 -11.954 1.00 19.42 ATOM 4124 O SER 574 32.129 8.135 -11.518 1.00 20.80 ATOM 4125 N THR 575 30.594 9.292 -12.694 1.00 17.84 ATOM 4126 CA THR 575 29.802 8.107 -13.017 1.00 20.27 ATOM 4127 CB THR 575 28.302 8.391 -13.007 1.00 16.07 ATOM 4128 OG1 THR 575 28.007 9.424 -13.948 1.00 22.01 ATOM 4129 CG2 THR 575 27.875 8.857 -11.661 1.00 20.62 ATOM 4130 C THR 575 30.138 7.475 -14.364 1.00 26.24 ATOM 4131 O THR 575 29.468 6.511 -14.758 1.00 32.16 ATOM 4132 N THR 576 31.146 8.009 -15.065 1.00 25.53 ATOM 4133 CA THR 576 31.574 7.489 -16.365 1.00 28.39 ATOM 4134 CB THR 576 30.923 8.210 -17.577 1.00 31.77 ATOM 4135 OG1 THR 576 30.795 9.612 -17.303 1.00 31.40 ATOM 4136 CG2 THR 576 29.604 7.570 -17.985 1.00 34.68 ATOM 4137 C THR 576 33.029 7.746 -16.597 1.00 29.87 ATOM 4138 O THR 576 33.623 8.601 -15.950 1.00 34.81 ATOM 4139 N ASN 577 33.585 7.029 -17.567 1.00 31.68 ATOM 4140 CA ASN 577 34.965 7.234 -17.962 1.00 32.54 ATOM 4141 CB ASN 577 35.513 6.018 -18.723 1.00 38.35 ATOM 4142 CG ASN 577 35.575 4.757 -17.863 1.00 45.89 ATOM 4143 OD1 ASN 577 34.795 4.587 -16.924 1.00 53.01 ATOM 4144 ND2 ASN 577 36.505 3.863 -18.185 1.00 47.10 ATOM 4145 C ASN 577 34.830 8.438 -18.898 1.00 29.69 ATOM 4146 O ASN 577 33.765 8.651 -19.490 1.00 29.69 ATOM 4147 N LEU 578 35.876 9.243 -18.999 1.00 25.93 ATOM 4148 CA LEU 578 35.851 10.419 -19.856 1.00 24.60 ATOM 4149 CB LEU 578 34.984 11.510 -19.216 1.00 24.64 ATOM 4150 CG LEU 578 34.712 12.813 -19.972 1.00 22.62 ATOM 4151 CD1 LEU 578 33.537 12.583 -20.895 1.00 27.61 ATOM 4152 CD2 LEU 578 34.365 13.949 -19.023 1.00 21.47 ATOM 4153 C LEU 578 37.278 10.923 -19.968 1.00 24.35 ATOM 4154 O LEU 578 38.134 10.526 -19.191 1.00 29.74 ATOM 4155 N ARG 579 37.560 11.745 -20.963 1.00 22.26 ATOM 4156 CA ARG 579 38.888 12.318 -21.086 1.00 20.20 ATOM 4157 CB ARG 579 39.371 12.315 -22.528 1.00 22.68 ATOM 4158 CG ARG 579 39.639 10.946 -23.095 1.00 28.06 ATOM 4159 CD ARG 579 40.144 11.045 -24.534 1.00 27.95 ATOM 4160 NE ARG 579 39.100 11.464 -25.456 1.00 26.06 ATOM 4161 CZ ARG 579 39.351 12.036 -26.621 1.00 27.53 ATOM 4162 NH1 ARG 579 40.606 12.248 -26.993 1.00 28.69 ATOM 4163 NH2 ARG 579 38.354 12.417 -27.401 1.00 29.94 ATOM 4164 C ARG 579 38.750 13.752 -20.664 1.00 18.59 ATOM 4165 O ARG 579 37.763 14.411 -20.995 1.00 20.40 ATOM 4166 N LEU 580 39.721 14.235 -19.920 1.00 19.86 ATOM 4167 CA LEU 580 39.738 15.617 -19.481 1.00 23.93 ATOM 4168 CB LEU 580 39.916 15.744 -17.970 1.00 28.52 ATOM 4169 CG LEU 580 38.899 15.198 -16.973 1.00 28.66 ATOM 4170 CD1 LEU 580 39.238 15.819 -15.627 1.00 34.80 ATOM 4171 CD2 LEU 580 37.484 15.569 -17.365 1.00 29.91 ATOM 4172 C LEU 580 40.984 16.140 -20.148 1.00 25.88 ATOM 4173 O LEU 580 41.891 15.363 -20.481 1.00 28.77 ATOM 4174 N PHE 581 41.051 17.445 -20.334 1.00 24.42 ATOM 4175 CA PHE 581 42.207 18.039 -20.982 1.00 23.21 ATOM 4176 CB PHE 581 41.802 18.666 -22.324 1.00 23.26 ATOM 4177 CG PHE 581 40.999 17.757 -23.193 1.00 23.59 ATOM 4178 CD1 PHE 581 39.694 18.090 -23.540 1.00 24.13 ATOM 4179 CD2 PHE 581 41.528 16.541 -23.623 1.00 21.60 ATOM 4180 CE1 PHE 581 38.917 17.225 -24.294 1.00 17.92 ATOM 4181 CE2 PHE 581 40.766 15.668 -24.375 1.00 20.87 ATOM 4182 CZ PHE 581 39.452 16.007 -24.711 1.00 20.99 ATOM 4183 C PHE 581 42.719 19.128 -20.092 1.00 18.97 ATOM 4184 O PHE 581 41.943 19.854 -19.505 1.00 21.90 ATOM 4185 N VAL 582 44.023 19.212 -19.942 1.00 21.20 ATOM 4186 CA VAL 582 44.601 20.274 -19.151 1.00 24.84 ATOM 4187 CB VAL 582 45.280 19.739 -17.894 1.00 27.84 ATOM 4188 CG1 VAL 582 45.931 20.889 -17.126 1.00 26.34 ATOM 4189 CG2 VAL 582 44.247 18.998 -17.019 1.00 30.24 ATOM 4190 C VAL 582 45.579 20.970 -20.079 1.00 25.68 ATOM 4191 O VAL 582 46.323 20.322 -20.792 1.00 23.96 ATOM 4192 N GLN 583 45.499 22.291 -20.129 1.00 31.11 ATOM 4193 CA GLN 583 46.341 23.103 -20.995 1.00 30.37 ATOM 4194 CB GLN 583 45.485 23.732 -22.078 1.00 37.03 ATOM 4195 CG GLN 583 44.573 22.758 -22.772 1.00 46.47 ATOM 4196 CD GLN 583 43.483 23.449 -23.566 1.00 49.92 ATOM 4197 OE1 GLN 583 42.307 23.070 -23.475 1.00 54.21 ATOM 4198 NE2 GLN 583 43.856 24.471 -24.340 1.00 43.85 ATOM 4199 C GLN 583 46.903 24.236 -20.188 1.00 27.68 ATOM 4200 O GLN 583 46.271 24.679 -19.247 1.00 27.53 ATOM 4201 N ASN 584 48.074 24.722 -20.565 1.00 25.21 ATOM 4202 CA ASN 584 48.667 25.839 -19.862 1.00 25.95 ATOM 4203 CB ASN 584 49.861 25.395 -19.017 1.00 27.68 ATOM 4204 CG ASN 584 51.060 25.037 -19.837 1.00 24.49 ATOM 4205 OD1 ASN 584 50.977 24.927 -21.044 1.00 28.26 ATOM 4206 ND2 ASN 584 52.197 24.858 -19.181 1.00 25.26 ATOM 4207 C ASN 584 49.059 26.829 -20.945 1.00 28.49 ATOM 4208 O ASN 584 48.928 26.500 -22.129 1.00 29.88 ATOM 4209 N SER 585 49.496 28.036 -20.579 1.00 27.45 ATOM 4210 CA SER 585 49.875 29.035 -21 596 1.00 30.77 ATOM 4211 CB SER 585 49.765 30.456 -21.039 1.00 29.03 ATOM 4212 OG SER 585 50.325 30.548 -19.741 1.00 34.88 ATOM 4213 C SER 585 51.253 28.811 -22.246 1.00 34.38 ATOM 4214 O SER 585 51.708 29.622 -23.057 1.00 31.24 ATOM 4215 N ASN 586 51.899 27.703 -21.867 1.00 37.42 ATOM 4216 CA ASN 586 53.203 27.294 -22.371 1.00 35.38 ATOM 4217 CB ASN 586 53.971 26.624 -21.236 1.00 41.48 ATOM 4218 CG ASN 586 55.458 26.554 -21.491 1.00 47.03 ATOM 4219 OD1 ASN 586 56.116 25.553 -21.166 1.00 53.23 ATOM 4220 ND2 ASN 586 56.012 27.626 -22.041 1.00 48.92 ATOM 4221 C ASN 586 52.915 26.292 -23.494 1.00 37.30 ATOM 4222 O ASN 586 53.795 25.601 -23.990 1.00 40.09 ATOM 4223 N ASN 587 51.641 26.196 -23.852 1.00 37.02 ATOM 4224 CA ASN 587 51.159 25.321 -24.903 1.00 36.39 ATOM 4225 CB ASN 587 51.752 25.738 -26.243 1.00 39.55 ATOM 4226 CG ASN 587 51.245 27.096 -26.691 1.00 44.89 ATOM 4227 OD1 ASN 587 50.047 27.283 -26.893 1.00 46.33 ATOM 4228 ND2 ASN 587 52.148 28.064 -26.807 1.00 48.96 ATOM 4229 C ASN 587 51.285 23.826 -24.668 1.00 35.84 ATOM 4230 O ASN 587 51.377 23.051 -25.616 1.00 37.37 ATOM 4231 N ASP 588 51.315 23.415 -23.405 1.00 32.62 ATOM 4232 CA ASP 588 51.367 21.994 -23.085 1.00 27.76 ATOM 4233 CB ASP 588 51.890 21.743 -21.662 1.00 27.66 ATOM 4234 CG ASP 588 53.360 22.117 -21.482 1.00 32.14 ATOM 4235 OD1 ASP 588 54.196 21.764 -22.342 1.00 34.35 ATOM 4236 OD2 ASP 588 53.689 22.743 -20.448 1.00 37.89 ATOM 4237 C ASP 588 49.898 21.604 -23.153 1.00 24.16 ATOM 4238 O ASP 588 49.042 22.424 -22.859 1.00 29.81 ATOM 4239 N PHE 589 49.601 20.378 -23.561 1.00 22.69 ATOM 4240 CA PHE 589 48.233 19.911 -23.653 1.00 19.26 ATOM 4241 CB PHE 589 47.781 19.909 -25.115 1.00 19.07 ATOM 4242 CG PHE 589 46.329 19.561 -25.308 1.00 17.33 ATOM 4243 CD1 PHE 589 45.382 20.555 -25.464 1.00 13.39 ATOM 4244 CD2 PHE 589 45.913 18.242 -25.294 1.00 14.50 ATOM 4245 CE1 PHE 589 44.041 20.230 -25.595 1.00 14.12 ATOM 4246 CE2 PHE 589 44.581 17.923 -25.426 1.00 16.69 ATOM 4247 CZ PHE 589 43.645 18.923 -25.576 1.00 13.30 ATOM 4248 C PHE 589 48.277 18.496 -23.113 1.00 24.44 ATOM 4249 O PHE 589 48.926 17.640 -23.703 1.00 27.71 ATOM 4250 N LEU 590 47.610 18.239 -21.991 1.00 26.31 ATOM 4251 CA LEU 590 47.632 16.907 -21.393 1.00 24.82 ATOM 4252 CB LEU 590 48.088 16.974 -19.927 1.00 31.03 ATOM 4253 CG LEU 590 49.371 17.763 -19.647 1.00 34.58 ATOM 4254 CD1 LEU 590 49.688 17.755 -18.166 1.00 39.41 ATOM 4255 CD2 LEU 590 50.529 17.193 -20.440 1.00 40.80 ATOM 4256 C LEU 590 46.264 16.285 -21.475 1.00 22.29 ATOM 4257 O LEU 590 45.268 16.965 -21.365 1.00 24.04 ATOM 4258 N VAL 591 46.220 14.983 -21.670 1.00 21.66 ATOM 4259 CA VAL 591 44.955 14.302 -21.773 1.00 24.60 ATOM 4260 CB VAL 591 44.860 13.505 -23.076 1.00 25.35 ATOM 4261 CG1 VAL 591 43.700 12.514 -23.01 1.00 25.77 ATOM 4262 CG2 VAL 591 44.694 14.474 -24.248 1.00 25.42 ATOM 4263 C VAL 591 44.873 13.383 -20.599 1.00 29.13 ATOM 4264 O VAL 591 45.784 12.564 -20.389 1.00 34.66 ATOM 4265 N ILE 592 43.773 13.510 -19.851 1.00 29.73 ATOM 4266 CA ILE 592 43.530 12.726 -18.640 1.00 23.90 ATOM 4267 CB ILE 592 43.552 13.666 -17.407 1.00 21.74 ATOM 4268 CG2 ILE 592 43.189 12.927 -16.148 1.00 16.67 ATOM 4269 CG1 ILE 592 44.940 14.319 -17.319 1.00 19.32 ATOM 4270 CD1 ILE 592 45.293 14.941 -15.995 1.00 24.87 ATOM 4271 C ILE 592 42.245 11.903 -18.715 1.00 21.42 ATOM 4272 O ILE 592 41.171 12.448 -18.843 1.00 19.52 ATOM 4273 N TYR 593 42.380 10.580 -18.684 1.00 22.86 ATOM 4274 CA TYR 593 41.242 9.680 -18.751 1.00 26.10 ATOM 4275 CB TYR 593 41.630 8.313 -19.346 1.00 34.27 ATOM 4276 CG TYR 593 42.224 8.392 -20.722 1.00 43.75 ATOM 4277 CD1 TYR 593 43.577 8.706 -20.903 1.00 47.60 ATOM 4278 CE1 TYR 593 44.120 8.903 -22.183 1.00 51.15 ATOM 4279 CD2 TYR 593 41.419 8.257 -21.854 1.00 51.36 ATOM 4280 CE2 TYR 593 41.951 8.450 -23.147 1.00 54.75 ATOM 4281 CZ TYR 593 43.300 8.780 -23.301 1.00 56.25 ATOM 4282 OH TYR 593 43.805 9.043 -24.569 1.00 63.62 ATOM 4283 C TYR 593 40.806 9.431 -17.344 1.00 27.01 ATOM 4284 O TYR 593 41.552 8.843 -16.581 1.00 30.49 ATOM 4285 N ILE 594 39.633 9.918 -16.971 1.00 28.13 ATOM 4286 CA ILE 594 39.126 9.668 -15.640 1.00 24.97 ATOM 4287 CB ILE 594 38.397 10.914 -15.060 1.00 26.87 ATOM 4288 CG2 ILE 594 39.366 12.111 -15.052 1.00 24.59 ATOM 4289 CG1 ILE 594 37.127 11.250 -15.855 1.00 25.95 ATOM 4290 CD1 ILE 594 36.068 12.055 -15.092 1.00 20.64 ATOM 4291 C ILE 594 38.236 8.425 -15.778 1.00 26.39 ATOM 4292 O ILE 594 37.811 8.087 -16.886 1.00 29.00 ATOM 4293 N ASN 595 38.083 7.658 -14.703 1.00 28.31 ATOM 4294 CA ASN 595 37.256 6.446 -14.731 1.00 27.72 ATOM 4295 CB ASN 595 38.030 5.188 -14.310 1.00 30.83 ATOM 4296 CG ASN 595 39.106 4.793 -15.305 1.00 32.89 ATOM 4297 OD1 ASN 595 40.238 5.267 -15.224 1.00 36.90 ATOM 4298 ND2 ASN 595 38.770 3.900 -16.225 1.00 33.97 ATOM 4299 C ASN 595 36.075 6.583 -13.807 1.00 28.15 ATOM 4300 O ASN 595 36.057 7.435 -12.909 1.00 27.50 ATOM 4301 N LYS 596 35.107 5.701 -14.021 1.00 27.21 ATOM 4302 CA LYS 596 33.883 5.672 -13.244 1.00 25.84 ATOM 4303 CB LYS 596 32.955 4.603 -13.805 1.00 24.28 ATOM 4304 CG LYS 596 31.686 4.499 -13.047 1.00 24.79 ATOM 4305 CD LYS 596 30.841 3.335 -13.480 1.00 28.00 ATOM 4306 CE LYS 596 29.412 3.630 -13.058 1.00 28.21 ATOM 4307 NZ LYS 596 28.558 2.421 -13.029 1.00 39.48 ATOM 4308 C LYS 596 34.231 5.304 -11.819 1.00 26.80 ATOM 4309 O LYS 596 34.908 4.308 -11.599 1.00 33.76 ATOM 4310 N THR 597 33.764 6.075 -10.848 1.00 23.21 ATOM 4311 CA THR 597 34.057 5.755 -9.465 1.00 19.85 ATOM 4312 CB THR 597 34.832 6.899 -8.789 1.00 17.47 ATOM 4313 OG1 THR 597 34.170 8.134 -9.045 1.00 23.13 ATOM 4314 CG2 THR 597 36.252 7.008 -9.346 1.00 20.56 ATOM 4315 C THR 597 32.796 5.445 -8.660 1.00 23.42 ATOM 4316 O THR 597 32.881 4.846 -7.583 1.00 25.02 ATOM 4317 N MET 598 31.626 5.762 -9.217 1.00 24.63 ATOM 4318 CA MET 598 30.350 5.574 -8.508 1.00 29.69 ATOM 4319 CB MET 598 30.064 6.832 -7.678 1.00 31.74 ATOM 4320 CG MET 598 30.027 8.092 -8.549 1.00 36.11 ATOM 4321 SD MET 598 29.755 9.702 -7.775 1.00 37.36 ATOM 4322 CE MET 598 27.948 9.542 -7.233 1.00 43.52 ATOM 4323 C MET 598 29.201 5.415 -9.479 1.00 28.31 ATOM 4324 O MET 598 29.351 5.702 -10.642 1.00 36.08 ATOM 4325 N ASN 599 28.046 4.978 -9.015 1.00 29.59 ATOM 4326 CA ASN 599 26.909 4.878 -9.914 1.00 34.34 ATOM 4327 CB ASN 599 26.040 3.662 -9.612 1.00 36.17 ATOM 4328 CG ASN 599 26.744 2.360 -9.880 1.00 37.88 ATOM 4329 OD1 ASN 599 27.835 2.326 -10.422 1.00 44.96 ATOM 4330 ND2 ASN 599 26.124 1.271 -9.484 1.00 46.10 ATOM 4331 C ASN 599 26.129 6.147 -9.654 1.00 38.09 ATOM 4332 O ASN 599 26.335 6.794 -8.638 1.00 42.60 ATOM 4333 N LYS 600 25.187 6.470 -10.525 1.00 43.32 ATOM 4334 CA LYS 600 24.405 7.696 -10.380 1.00 46.30 ATOM 4335 CB LYS 600 23.445 7.836 -11.562 1.00 52.15 ATOM 4336 CG LYS 600 24.108 7.719 -12.922 1.00 58.49 ATOM 4337 CD LYS 600 23.111 7.956 -14.047 1.00 64.43 ATOM 4338 CE LYS 600 23.755 7.665 -15.395 1.00 69.24 ATOM 4339 NZ LYS 600 22.804 7.771 -16.540 1.00 75.49 ATOM 4340 C LYS 600 23.622 7.799 -9.077 1.00 46.95 ATOM 4341 O LYS 600 23.478 8.882 -8.502 1.00 46.03 ATOM 4342 N ASP 601 23.092 6.662 -8.642 1.00 49.46 ATOM 4343 CA ASP 601 22.289 6.577 -7.425 1.00 49.50 ATOM 4344 CB ASP 601 21.352 5.366 -7.507 1.00 50.83 ATOM 4345 CG ASP 601 22.079 4.065 -7.887 1.00 55.52 ATOM 4346 OD1 ASP 601 21.381 3.044 -8.093 1.00 57.44 ATOM 4347 OD2 ASP 601 23.330 4.050 -7.985 1.00 53.34 ATOM 4348 C ASP 601 23.130 6.516 -6.152 1.00 50.82 ATOM 4349 O ASP 601 22.613 6.263 -5.055 1.00 54.21 ATOM 4350 N ASP 602 24.434 6.710 -6.302 1.00 48.64 ATOM 4351 CA ASP 602 25.330 6.691 -5.159 1.00 44.01 ATOM 4352 CB ASP 602 26.717 6.214 -5.575 1.00 40.23 ATOM 4353 CG ASP 602 26.791 4.738 -5.737 1.00 37.25 ATOM 4354 OD1 ASP 602 27.816 4.259 -6.264 1.00 36.68 ATOM 4355 OD2 ASP 602 25.833 4.054 -5.321 1.00 42.23 ATOM 4356 C ASP 602 25.467 8.073 -4.558 1.00 44.20 ATOM 4357 O ASP 602 25.306 9.086 -5.248 1.00 45.97 ATOM 4358 N ASP 603 25.764 8.107 -3.265 1.00 43.46 ATOM 4359 CA ASP 603 25.978 9.361 -2.571 1.00 38.92 ATOM 4360 CB ASP 603 25.448 9.294 -1.135 1.00 48.43 ATOM 4361 CG ASP 603 23.964 9.623 -1.042 1.00 58.48 ATOM 4362 OD1 ASP 603 23.139 8.684 -1.123 1.00 62.56 ATOM 4363 OD2 ASP 603 23.626 10.824 -0.878 1.00 63.75 ATOM 4364 C ASP 603 27.477 9.613 -2.573 1.00 31.62 ATOM 4365 O ASP 603 28.274 8.688 -2.729 1.00 23.41 ATOM 4366 N LEU 604 27.842 10.881 -2.448 1.00 28.74 ATOM 4367 CA LEU 604 29.226 11.278 -2.422 1.00 27.24 ATOM 4368 CB LEU 604 29.357 12.764 -2.664 1.00 22.42 ATOM 4369 CG LEU 604 29.148 13.160 -4.095 1.00 19.01 ATOM 4370 CD1 LEU 604 29.691 14.557 -4.260 1.00 22.34 ATOM 4371 CD2 LEU 604 29.876 12.206 -4.987 1.00 23.64 ATOM 4372 C LEU 604 29.915 10.933 -1.117 1.00 26.64 ATOM 4373 O LEU 604 29.977 11.739 -0.206 1.00 30.89 ATOM 4374 N THR 605 30.398 9.713 -1.020 1.00 27.07 ATOM 4375 CA THR 605 31.118 9.302 0.160 1.00 27.67 ATOM 4376 CB THR 605 30.660 7.934 0.637 1.00 26.78 ATOM 4377 OG1 THR 605 30.956 6.950 -0.361 1.00 35.48 ATOM 4378 CG2 THR 605 29.155 7.972 0.902 1.00 28.06 ATOM 4379 C THR 605 32.613 9.291 -0.151 1.00 26.21 ATOM 4380 O THR 605 33.032 9.490 -1.307 1.00 26.25 ATOM 4381 N TYR 606 33.416 9.058 0.879 1.00 24.88 ATOM 4382 CA TYR 606 34.852 9.038 0.722 1.00 21.81 ATOM 4383 CB TYR 606 35.530 8.580 2.010 1.00 19.51 ATOM 4384 CG TYR 606 37.025 8.692 1.931 1.00 19.63 ATOM 4385 CD1 TYR 606 37.659 9.942 2.019 1.00 19.75 ATOM 4386 CE1 TYR 606 39.032 10.068 1.821 1.00 17.57 ATOM 4387 CD2 TYR 606 37.806 7.566 1.655 1.00 16.29 ATOM 4388 CE2 TYR 606 39.176 7.674 1.457 1.00 16.64 ATOM 4389 CZ TYR 606 39.782 8.923 1.544 1.00 18.29 ATOM 4390 OH TYR 606 41.144 9.001 1.411 1.00 23.20 ATOM 4391 C TYR 606 35.281 8.184 -0.471 1.00 23.40 ATOM 4392 O TYR 606 35.921 8.691 -1.389 1.00 22.13 ATOM 4393 N GLN 607 34.870 6.924 -0.509 1.00 27.60 ATOM 4394 CA GLN 607 35.250 6.036 -1.607 1.00 29.41 ATOM 4395 CB GLN 607 34.811 4.594 -1.320 1.00 37.18 ATOM 4396 CG GLN 607 33.310 4.398 -1.147 1.00 50.31 ATOM 4397 CD GLN 607 32.949 2.961 -0.777 1.00 59.10 ATOM 4398 OE1 GLN 607 33.005 2.048 -1.610 1.00 66.18 ATOM 4399 NE2 GLN 607 32.595 2.752 0.483 1.00 64.92 ATOM 4400 C GLN 607 34.832 6.451 -3.027 1.00 29.69 ATOM 4401 O GLN 607 35.347 5.892 -4.005 1.00 33.55 ATOM 4402 N THR 608 33.935 7.430 -3.167 1.00 26.45 ATOM 4403 CA THR 608 33.535 7.861 -4.512 1.00 22.19 ATOM 4404 CB THR 608 32.188 8.600 -4.519 1.00 18.19 ATOM 4405 OG1 THR 608 32.268 9.728 -3.649 1.00 22.75 ATOM 4406 CG2 THR 608 31.052 7.685 -4.072 1.00 15.16 ATOM 4407 C THR 608 34.596 8.751 -5.200 1.00 24.93 ATOM 4408 O THR 608 34.521 8.982 -6.403 1.00 30.46 ATOM 4409 N PHE 609 35.547 9.301 -4.450 1.00 20.11 ATOM 4410 CA PHE 609 36.575 10.116 -5.073 1.00 17.66 ATOM 4411 CB PHE 609 36.904 11.346 -4.251 1.00 16.23 ATOM 4412 CG PHE 609 35.841 12.399 -4.296 1.00 15.72 ATOM 4413 CD1 PHE 609 34.710 12.290 -3.510 1.00 14.16 ATOM 4414 CD2 PHE 609 36.012 13.537 -5.062 1.00 19.17 ATOM 4415 CE1 PHE 609 33.785 13.285 -3.467 1.00 13.99 ATOM 4416 CE2 PHE 609 35.080 14.554 -5.031 1.00 17.80 ATOM 4417 CZ PHE 609 33.965 14.430 -4.226 1.00 19.15 ATOM 4418 C PHE 609 37.822 9.306 -5.368 1.00 17.82 ATOM 4419 O PHE 609 38.097 8.300 -4.704 1.00 18.54 ATOM 4420 N ASP 610 38.589 9.760 -6.354 1.00 16.24 ATOM 4421 CA ASP 610 39.774 9.048 -6.783 1.00 17.82 ATOM 4422 CB ASP 610 39.332 7.956 -7.763 1.00 28.02 ATOM 4423 CG ASP 610 40.381 6.868 -7.980 1.00 30.47 ATOM 4424 OD1 ASP 610 40.134 5.962 -8.812 1.00 36.74 ATOM 4425 OD2 ASP 610 41.442 6.910 -7.330 1.00 35.21 ATOM 4426 C ASP 610 40.746 10.006 -7.437 1.00 15.64 ATOM 4427 O ASP 610 40.479 11.198 -7.502 1.00 18.05 ATOM 4428 N LEU 611 41.888 9.489 -7.888 1.00 19.89 ATOM 4429 CA LEU 611 42.934 10.287 -8.539 1.00 22.31 ATOM 4430 CB LEU 611 44.226 10.295 -7.718 1.00 18.56 ATOM 4431 CG LEU 611 44.209 10.950 -6.347 1.00 20.61 ATOM 4432 CD1 LEU 611 45.472 10.479 -5.583 1.00 22.97 ATOM 4433 CD2 LEU 611 44.143 12.474 -6.485 1.00 16.32 ATOM 4434 C LEU 611 43.289 9.779 -9.923 1.00 24.26 ATOM 4435 O LEU 611 43.798 8.672 -10.070 1.00 28.19 ATOM 4436 N ALA 612 43.054 10.620 -10.922 1.00 26.15 ATOM 4437 CA ALA 612 43.367 10.303 -12.297 1.00 25.40 ATOM 4438 CB ALA 612 42.212 10.717 -13.206 1.00 18.53 ATOM 4439 C ALA 612 44.604 11.145 -12.583 1.00 26.87 ATOM 4440 O ALA 612 44.722 12.255 -12.073 1.00 29.03 ATOM 4441 N THR 613 45.563 10.589 -13.316 1.00 30.85 ATOM 4442 CA THR 613 46.790 11.306 -13.677 1.00 30.80 ATOM 4443 CB THR 613 47.954 11.021 -12.682 1.00 31.03 ATOM 4444 OG1 THR 613 49.138 11.733 -13.085 1.00 30.18 ATOM 4445 CG2 THR 613 48.230 9.526 -12.581 1.00 26.60 ATOM 4446 C THR 613 47.203 10.922 -15.095 1.00 32.15 ATOM 4447 O THR 613 46.509 10.148 -15.777 1.00 28.30 ATOM 4448 N THR 614 48.293 11.511 -15.559 1.00 33.49 ATOM 4449 CA THR 614 48.793 11.217 -16.885 1.00 37.88 ATOM 4450 CB THR 614 48.422 12.345 -17.907 1.00 39.76 ATOM 4451 OG1 THR 614 48.954 12.044 -19.206 1.00 41.06 ATOM 4452 CG2 THR 614 48.905 13.698 -17.434 1.00 37.77 ATOM 4453 C THR 614 50.285 11.049 -16.701 1.00 41.10 ATOM 4454 O THR 614 50.842 11.420 -15.662 1.00 41.53 ATOM 4455 N ASN 615 50.925 10.411 -17.662 1.00 45.48 ATOM 4456 CA ASN 615 52.356 10.191 -17.563 1.00 50.76 ATOM 4457 CB ASN 615 52.724 8.742 -17.888 1.00 56.94 ATOM 4458 CG ASN 615 51.730 8.072 -18.820 1.00 64.66 ATOM 4459 OD1 ASN 615 50.839 8.714 -19.386 1.00 70.36 ATOM 4460 ND2 ASN 615 51.861 6.759 -18.964 1.00 69.92 ATOM 4461 C ASN 615 53.157 11.179 -18.397 1.00 52.54 ATOM 4462 O ASN 615 54.353 10.975 -18.645 1.00 58.56 ATOM 4463 N SER 616 52.491 12.244 -18.838 1.00 47.84 ATOM 4464 CA SER 616 53.146 13.299 -19.602 1.00 43.54 ATOM 4465 CB SER 616 52.307 13.715 -20.805 1.00 43.84 ATOM 4466 G SER 616 51.844 12.577 -21.512 1.00 54.32 ATOM 4467 C SER 616 53.147 14.417 -18.589 1.00 40.19 ATOM 4468 O SER 616 52.263 14.471 -17.742 1.00 42.93 ATOM 4469 N ASN 617 54.150 15.273 -18.617 1.00 37.04 ATOM 4470 CA ASN 617 54.177 16.358 -17.663 1.00 35.69 ATOM 4471 CB ASN 617 55.374 16.225 -16.707 1.00 37.96 ATOM 4472 CG ASN 617 56.672 15.997 -17.423 1.00 39.01 ATOM 4473 OD1 ASN 617 56.979 14.882 -17.808 1.00 43.35 ATOM 4474 ND2 ASN 617 57.455 17.044 -17.583 1.00 36.32 ATOM 4475 C ASN 617 54.119 17.732 -18.325 1.00 34.05 ATOM 4476 O ASN 617 54.092 17.853 -19.554 1.00 30.94 ATOM 4477 N MET 618 54.030 18.767 -17.500 1.00 33.24 ATOM 4478 CA MET 618 53.970 20.117 -18.013 1.00 33.10 ATOM 4479 CB MET 618 52.520 20.636 -18.025 1.00 32.29 ATOM 4480 CG MET 618 51.949 21.088 -16.702 1.00 29.92 ATOM 4481 SD MET 618 50.249 21.651 -16.931 1.00 30.97 ATOM 4482 CE MET 618 50.471 23.199 -16.787 1.00 32.23 ATOM 4483 C MET 618 54.921 21.078 -17.297 1.00 31.41 ATOM 4484 O MET 618 55.356 20.833 -16.165 1.00 31.17 ATOM 4485 N GLY 619 55.309 22.120 -18.018 1.00 27.75 ATOM 4486 CA GLY 619 56.210 23.112 -17.481 1.00 27.31 ATOM 4487 C GLY 619 55.584 24.468 -17.688 1.00 27.73 ATOM 4488 O GLY 619 54.616 24.605 -18.457 1.00 23.45 ATOM 4489 N PHE 620 56.173 25.472 -17.046 1.00 32.05 ATOM 4490 CA PHE 620 55.670 26.836 -17.087 1.00 34.44 ATOM 4491 CB PHE 620 55.100 27.179 -15.715 1.00 33.94 ATOM 4492 CG PHE 620 53.926 26.321 -15.312 1.00 28.19 ATOM 4493 CD1 PHE 620 54.124 25.157 -14.594 1.00 26.00 ATOM 4494 CD2 PHE 620 52.626 26.704 -15.632 1.00 28.04 ATOM 4495 CE1 PHE 620 53.063 24.389 -14.199 1.00 27.86 ATOM 4496 CE2 PHE 620 51.545 25.945 -15.237 1.00 24.13 ATOM 4497 CZ PHE 620 51.762 24.786 -14.518 1.00 29.09 ATOM 4498 C PHE 620 56.743 27.854 -17.445 1.00 40.11 ATOM 4499 O PHE 620 57.936 27.577 -17.300 1.00 43.33 ATOM 4500 N SER 621 56.317 29.042 -17.877 1.00 46.66 ATOM 4501 CA SER 621 57.239 30.115 -18.269 1.00 53.27 ATOM 4502 CB SER 621 57.435 30.146 -19.794 1.00 53.87 ATOM 4503 OG SER 621 58.551 29.390 -20.252 1.00 59.49 ATOM 4504 C SER 621 56.763 31.502 -17.826 1.00 56.51 ATOM 4505 O SER 621 55.563 31.802 -17.846 1.00 56.27 ATOM 4506 N GLY 622 57.720 32.347 -17.453 1.00 58.36 ATOM 4507 CA GLY 622 57.412 33.705 -17.050 1.00 60.94 ATOM 4508 C GLY 622 56.503 33.879 -15.858 1.00 62.66 ATOM 4509 O GLY 622 56.282 32.946 -15.085 1.00 61.90 ATOM 4510 N ASP 623 55.975 35.092 -15.723 1.00 66.16 ATOM 4511 CA ASP 623 55.087 35.438 -14.618 1.00 70.95 ATOM 4512 CB ASP 623 55.539 36.754 -13.940 1.00 73.92 ATOM 4513 CG ASP 623 55.538 37.966 -14.885 1.00 79.61 ATOM 4514 OD1 ASP 623 55.879 37.814 -16.085 1.00 81.17 ATOM 4515 OD2 ASP 623 55.216 39.087 -14.406 1.00 81.72 ATOM 4516 C ASP 623 53.583 35.457 -14.972 1.00 71.09 ATOM 4517 O ASP 623 52.732 35.653 -14.091 1.00 71.06 ATOM 4518 N LYS 624 53.260 35.226 -16.247 1.00 69.73 ATOM 4519 CA LYS 624 51.864 35.193 -16.704 1.00 65.87 ATOM 4520 CB LYS 624 51.632 36.207 -17.838 1.00 71.81 ATOM 4521 CG LYS 624 52.482 35.977 -19.090 1.00 81.96 ATOM 4522 CD LYS 624 52.057 36.892 -20.248 1.00 88.09 ATOM 4523 CE LYS 624 52.741 36.515 -21.580 1.00 91.31 ATOM 4524 NZ LYS 624 52.259 37.339 -22.749 1.00 90.55 ATOM 4525 C LYS 624 51.448 33.764 -17.119 1.00 59.37 ATOM 4526 O LYS 624 51.266 33.448 -18.302 1.00 58.24 ATOM 4527 N ASN 625 51.314 32.906 -16.115 1.00 49.44 ATOM 4528 CA ASN 625 50.948 31.519 -16.317 1.00 43.23 ATOM 4529 CB ASN 625 51.789 30.642 -15.417 1.00 42.10 ATOM 4530 CG ASN 625 53.236 30.661 -15.816 1.00 40.84 ATOM 4531 OD1 ASN 625 53.650 29.911 -16.696 1.00 43.01 ATOM 4532 ND2 ASN 625 54.009 31.556 -15.215 1.00 39.55 ATOM 4533 C ASN 625 49.479 31.251 -16.093 1.00 39.80 ATOM 4534 O ASN 625 48.923 31.608 -15.064 1.00 39.13 ATOM 4535 N GLU 626 48.845 30.629 -17.075 1.00 36.93 ATOM 4536 CA GLU 626 47.423 30.335 -16.993 1.00 38.81 ATOM 4537 CB GLU 626 46.619 31.272 -17.915 1.00 43.39 ATOM 4538 CG GLU 626 47.131 32.752 -17.888 1.00 54.84 ATOM 4539 CD GLU 626 46.114 33.803 -17.389 1.00 56.51 ATOM 4540 OE1 GLU 626 44.916 33.718 -17.760 1.00 58.31 ATOM 4541 OE2 GLU 626 46.538 34.745 -16.664 1.00 56.35 ATOM 4542 C GLU 626 47.183 28.865 -17.313 1.00 34.04 ATOM 4543 O GLU 626 47.992 28.227 -17.991 1.00 28.90 ATOM 4544 N LEU 627 46.117 28.322 -16.734 1.00 33.32 ATOM 4545 CA LEU 627 45.757 26.925 -16.893 1.00 31.13 ATOM 4546 CB LEU 627 46.061 26.154 -15.584 1.00 28.96 ATOM 4547 CG LEU 627 46.022 24.613 -15.610 1.00 27.57 ATOM 4548 CD1 LEU 627 47.403 24.059 -15.709 1.00 22.93 ATOM 4549 CD2 LEU 627 45.351 24.073 -14.391 1.00 28.78 ATOM 4550 C LEU 627 44.271 26.838 -17.208 1.00 29.90 ATOM 4551 O LEU 627 43.467 27.467 -16.538 1.00 33.36 ATOM 4552 N ILE 628 43.912 26.083 -18.241 1.00 30.36 ATOM 4553 CA ILE 628 42.519 25.902 -18.620 1.00 25.02 ATOM 4554 CB ILE 628 42.269 26.290 -20.073 1.00 25.94 ATOM 4555 CG2 ILE 628 40.813 26.445 -20.299 1.00 34.05 ATOM 4556 CG1 ILE 628 43.022 27.565 -20.466 1.00 27.41 ATOM 4557 CD1 ILE 628 42.755 28.745 -19.614 1.00 29.63 ATOM 4558 C ILE 628 42.263 24.411 -18.541 1.00 26.03 ATOM 4559 O ILE 628 43.131 23.609 -18.886 1.00 28.68 ATOM 4560 N ILE 629 41.090 24.033 -18.057 1.00 28.18 ATOM 4561 CA ILE 629 40.700 22.627 -17.960 1.00 25.83 ATOM 4562 CB ILE 629 40.135 22.262 -16.550 1.00 29.86 ATOM 4563 CG2 ILE 629 39.803 20.774 -16.463 1.00 32.13 ATOM 4564 CG1 ILE 629 41.152 22.594 -15.466 1.00 36.05 ATOM 4565 CD1 ILE 629 42.503 21.916 -15.642 1.00 41.73 ATOM 4566 C ILE 629 39.561 22.478 -18.967 1.00 23.61 ATOM 4567 O ILE 629 38.693 23.343 -19.063 1.00 19.96 ATOM 4568 N GLY 630 39.558 21.396 -19.721 1.00 20.85 ATOM 4569 CA GLY 630 38.500 21.188 -20.682 1.00 23.85 ATOM 4570 C GLY 630 38.068 19.749 -20.561 1.00 23.37 ATOM 4571 O GLY 630 38.690 19.001 -19.823 1.00 24.82 ATOM 4572 N ALA 631 37.033 19.350 -21.286 1.00 20.81 ATOM 4573 CA ALA 631 36.569 17.982 -21.226 1.00 23.26 ATOM 4574 CB ALA 631 35.565 17.804 -20.091 1.00 20.73 ATOM 4575 C ALA 631 35.916 17.661 -22.557 1.00 27.62 ATOM 4576 O ALA 631 35.650 18.556 -23.356 1.00 29.95 ATOM 4577 N GLU 632 35.732 16.377 -22.829 1.00 31.92 ATOM 4578 CA GLU 632 35.078 15.963 -24.059 1.00 32.85 ATOM 4579 CB GLU 632 35.650 14.644 -24.570 1.00 31.26 ATOM 4580 CG GLU 632 35.053 13.414 -23.921 1.00 27.95 ATOM 4581 CD GLU 632 35.713 12.143 -24.385 1.00 36.80 ATOM 4582 OE1 GLU 632 36.369 12.154 -25.451 1.00 40.53 ATOM 4583 OE2 GLU 632 35.590 11.123 -23.678 1.00 41.05 ATOM 4584 C GLU 632 33.625 15.776 -23.674 1.00 33.61 ATOM 4585 O GLU 632 33.280 15.718 -22.494 1.00 38.27 ATOM 4586 N SER 633 32.788 15.582 -24.665 1.00 32.84 ATOM 4587 CA SER 633 31.371 15.420 -24.418 1.00 35.35 ATOM 4588 CB SER 633 30.627 15.688 -25.723 1.00 38.12 ATOM 4589 OG SER 633 30.955 16.994 -26.189 1.00 46.45 ATOM 4590 C SER 633 30.937 14.092 -23.809 1.00 34.15 ATOM 4591 O SER 633 31.566 13.058 -24.025 1.00 35.25 ATOM 4592 N PHE 634 29.839 14.135 -23.064 1.00 34.80 ATOM 4593 CA PHE 634 29.262 12.960 -22.419 1.00 37.23 ATOM 4594 CB PHE 634 29.754 12.854 -20.976 1.00 34.83 ATOM 4595 CG PHE 634 29.346 14.010 -20.117 1.00 30.25 ATOM 4596 CD1 PHE 634 28.262 13.895 -19.245 1.00 28.96 ATOM 4597 CD2 PHE 634 30.016 15.226 -20.203 1.00 27.74 ATOM 4598 CE1 PHE 634 27.846 14.974 -18.475 1.00 24.91 ATOM 4599 CE2 PHE 634 29.610 16.314 -19.437 1.00 29.50 ATOM 4600 CZ PHE 634 28.520 16.187 -18.571 1.00 25.99 ATOM 4601 C PHE 634 27.746 13.173 -22.433 1.00 42.26 ATOM 4602 O PHE 634 27.280 14.313 -22.607 1.00 43.66 ATOM 4603 N VAL 635 26.969 12.105 -22.263 1.00 44.81 ATOM 4604 CA VAL 635 25.510 12.249 -22.268 1.00 49.75 ATOM 4605 CB VAL 635 24.773 10.914 -22.408 1.00 48.09 ATOM 4606 CG1 VAL 635 24.749 10.479 -23.868 1.00 54.19 ATOM 4607 CG2 VAL 635 25.427 9.860 -21.545 1.00 48.38 ATOM 4608 C VAL 635 25.045 12.875 -20.989 1.00 52.73 ATOM 4609 O VAL 635 25.668 12.694 -19.947 1.00 56.22 ATOM 4610 N SER 636 23.955 13.622 -21.064 1.00 56.71 ATOM 4611 CA SER 636 23.401 14.258 -19.876 1.00 60.84 ATOM 4612 CB SER 636 22.250 15.197 -20.266 1.00 66.55 ATOM 4613 OG SER 636 21.286 14.545 -21.094 1.00 74.32 ATOM 4614 C SER 636 22.925 13.169 -18.895 1.00 59.04 ATOM 4615 O SER 636 22.573 12.049 -19.303 1.00 58.56 ATOM 4616 N GLY 637 22.934 13.489 -17.605 1.00 55.58 ATOM 4617 CA GLY 637 22.523 12.511 -16.616 1.00 52.89 ATOM 4618 C GLY 637 23.713 11.817 -15.963 1.00 50.21 ATOM 4619 O GLY 637 23.534 10.968 -15.100 1.00 54.08 ATOM 4620 N GLU 638 24.924 12.120 -16.417 1.00 45.05 ATOM 4621 CA GLU 638 26.123 11.544 -15.830 1.00 38.98 ATOM 4622 CB GLU 638 27.134 11.150 -16.902 1.00 40.82 ATOM 4623 CG GLU 638 26.651 10.070 -17.846 1.00 41.29 ATOM 4624 CD GLU 638 26.536 8.713 -17.198 1.00 44.15 ATOM 4625 OE1 GLU 638 26.859 8.570 -16.008 1.00 51.56 ATOM 4626 OE2 GLU 638 26.140 7.758 -17.887 1.00 48.24 ATOM 4627 C GLU 638 26.694 12.632 -14.936 1.00 37.82 ATOM 4628 O GLU 638 26.748 13.809 -15.318 1.00 40.61 ATOM 4629 N LYS 639 27.078 12.246 -13.730 1.00 31.64 ATOM 4630 CA LYS 639 27.601 13.190 -12.765 1.00 25.56 ATOM 4631 CB LYS 639 27.080 12.853 -11.366 1.00 29.28 ATOM 4632 CG LYS 639 25.593 12.600 -11.246 1.00 34.14 ATOM 4633 CD LYS 639 25.316 11.994 -9.867 1.00 48.20 ATOM 4634 CE LYS 639 23.830 11.816 -9.571 1.00 50.33 ATOM 4635 NZ LYS 639 23.172 10.838 -10.481 1.00 57.45 ATOM 4636 C LYS 639 29.110 13.139 -12.733 1.00 20.16 ATOM 4637 O LYS 639 29.686 12.056 -12.594 1.00 21.41 ATOM 4638 N ILE 640 29.734 14.308 -12.856 1.00 16.72 ATOM 4639 CA ILE 640 31.177 14.457 -12.802 1.00 13.62 ATOM 4640 CB ILE 640 31.825 14.866 -14.158 1.00 13.79 ATOM 4641 CG2 ILE 640 33.295 15.154 -13.943 1.00 15.50 ATOM 4642 CG1 ILE 640 31.751 13.734 -15.191 1.00 13.55 ATOM 4643 CD1 ILE 640 30.610 13.831 -16.190 1.00 11.62 ATOM 4644 C ILE 640 31.418 15.572 -11.809 1.00 18.26 ATOM 4645 O ILE 640 30.845 16.646 -11.936 1.00 20.94 ATOM 4646 N TYR 641 32.210 15.288 -10.778 1.00 20.12 ATOM 4647 CA TYR 641 32.548 16.254 -9.741 1.00 17.06 ATOM 4648 CB TYR 641 32.093 15.736 -8.394 1.00 12.33 ATOM 4649 CG TYR 641 30.629 15.427 -8.353 1.00 19.71 ATOM 4650 CD1 TYR 641 30.170 14.134 -8.582 1.00 20.72 ATOM 4651 CE1 TYR 641 28.821 13.833 -8.508 1.00 25.35 ATOM 4652 CD2 TYR 641 29.697 16.421 -8.050 1.00 18.05 ATOM 4653 CE2 TYR 641 28.358 16.132 -7.968 1.00 26.09 ATOM 4654 CZ TYR 641 27.924 14.834 -8.191 1.00 24.94 ATOM 4655 OH TYR 641 26.597 14.530 -8.023 1.00 32.32 ATOM 4656 C TYR 641 34.060 16.389 -9.708 1.00 18.01 ATOM 4657 O TYR 641 34.779 15.391 -9.614 1.00 18.42 ATOM 4658 N ILE 642 34.550 17.606 -9.833 1.00 16.45 ATOM 4659 CA ILE 642 35.988 17.808 -9.791 1.00 20.87 ATOM 4660 CB ILE 642 36.491 18.575 -11.029 1.00 20.47 ATOM 4661 CG2 ILE 642 37.958 18.793 -10.911 1.00 20.81 ATOM 4662 CG1 ILE 642 36.235 17.760 -12.306 1.00 19.36 ATOM 4663 CD1 ILE 642 36.571 18.515 -13.566 1.00 21.85 ATOM 4664 C ILE 642 36.246 18.593 -8.512 1.00 20.68 ATOM 4665 O ILE 642 35.470 19.494 -8.187 1.00 22.38 ATOM 4666 N ASP 643 37.304 18.230 -7.783 1.00 20.18 ATOM 4667 CA ASP 643 37.655 18.879 -6.508 1.00 18.65 ATOM 4668 CB ASP 643 37.531 17.821 -5.382 1.00 22.35 ATOM 4669 CG ASP 643 38.028 18.294 -4.024 1.00 26.15 ATOM 4670 OD1 ASP 643 37.750 19.453 -3.625 1.00 25.20 ATOM 4671 OD2 ASP 643 38.684 17.464 -3.338 1.00 24.16 ATOM 4672 C ASP 643 39.030 19.587 -6.511 1.00 20.45 ATOM 4673 O ASP 643 39.096 20.821 -6.361 1.00 24.99 ATOM 4674 N LYS 644 40.116 18.842 -6.724 1.00 16.96 ATOM 4675 CA LYS 644 41.457 19.428 -6.714 1.00 17.58 ATOM 4676 CB LYS 644 42.246 18.997 -5.470 1.00 19.80 ATOM 4677 CG LYS 644 41.6&2 19.216 -4.117 1.00 22.38 ATOM 4678 CD LYS 644 41.412 20.668 -3.773 1.00 23.96 ATOM 4679 CE LYS 644 41.051 20.791 -2.310 1.00 20.00 ATOM 4680 NZ LYS 644 40.046 19.745 -1.948 1.00 20.46 ATOM 4681 C LYS 644 42.332 19.024 -7.884 1.00 18.74 ATOM 4682 O LYS 644 42.322 17.872 -8.296 1.00 21.48 ATOM 4683 N ILE 645 43.168 19.954 -8.329 1.00 17.54 ATOM 4684 CA ILE 645 44.132 19.717 -9.388 1.00 17.59 ATOM 4685 CB ILE 645 44.241 20.931 -10.352 1.00 21.58 ATOM 4686 CG2 ILE 645 45.150 20.602 -11.541 1.00 23.33 ATOM 4687 CG1 ILE 645 42.860 21.330 -10.878 1.00 25.80 ATOM 4688 CD1 ILE 645 42.170 20.258 -11.698 1.00 23.99 ATOM 4689 C ILE 645 45.416 19.643 -8.565 1.00 16.72 ATOM 4690 O ILE 645 45.684 20.540 -7.782 1.00 19.90 ATOM 4691 N GLU 646 46.185 18.568 -8.686 1.00 18.31 ATOM 4692 CA GLU 646 47.429 18.450 -7.922 1.00 16.72 ATOM 4693 CB GLU 646 47.459 17.158 -7.100 1.00 13.74 ATOM 4694 CG GLU 646 46.218 16.841 -6.292 1.00 11.87 ATOM 4695 CD GLU 646 46.475 15.711 -5.331 1.00 21.72 ATOM 4696 OE1 GLU 646 47.074 14.707 -5.762 1.00 22.74 ATOM 4697 OE2 GLU 646 46.104 15.822 -4.146 1.00 25.76 ATOM 4698 C GLU 646 48.679 18.501 -8.804 1.00 15.32 ATOM 4699 O GLU 646 48.728 17.894 -9.855 1.00 17.66 ATOM 4700 N PHE 647 49.701 19.198 -8.337 1.00 18.90 ATOM 4701 CA PHE 647 50.950 19.316 -9.060 1.00 20.74 ATOM 4702 CB PHE 647 51.299 20.783 -9.253 1.00 22.54 ATOM 4703 CG PHE 647 50.309 21.508 -10.096 1.00 16.80 ATOM 4704 CD1 PHE 647 49.263 22.185 -9.513 1.00 15.88 ATOM 4705 CD2 PHE 647 50.388 21.442 -11.474 1.00 15.98 ATOM 4706 CE1 PHE 647 48.297 22.779 -10.285 1.00 19.07 ATOM 4707 CE2 PHE 647 49.440 22.026 -12.251 1.00 17.20 ATOM 4708 CZ PHE 647 48.385 22.699 -11.658 1.00 21.92 ATOM 4709 C PHE 647 52.048 18.597 -8.327 1.00 23.01 ATOM 4710 O PHE 647 52.285 18.827 -7.145 1.00 25.26 ATOM 4711 N ILE 648 52.682 17.676 -9.032 1.00 27.24 ATOM 4712 CA ILE 648 53.766 16.884 -8.481 1.00 28.26 ATOM 4713 CB ILE 648 53.499 15.385 -8.728 1.00 28.25 ATOM 4714 CG2 ILE 648 54.433 14.542 -7.874 1.00 30.94 ATOM 4715 CG1 ILE 648 52.033 15.045 -8.428 1.00 26.62 ATOM 4716 CD1 ILE 648 51.634 13.616 -8.796 1.00 24.38 ATOM 4717 C ILE 648 55.009 17.299 -9.260 1.00 29.24 ATOM 4718 O ILE 648 54.979 17.314 -10.488 1.00 29.14 ATOM 4719 N PRO 649 56.079 17.735 -8.566 1.00 29.81 ATOM 4720 CD PRO 649 56.096 18.156 -7.167 1.00 26.84 ATOM 4721 CA PRO 649 57.323 18.153 -9.232 1.00 33.95 ATOM 4722 CB PRO 649 58.101 18.818 -8.111 1.00 25.42 ATOM 4723 CG PRO 649 57.039 19.324 -7.242 1.00 30.57 ATOM 4724 C PRO 649 58.075 16.947 -9.760 1.00 39.61 ATOM 4725 O PRO 649 58.648 16.186 -8.980 1.00 44.73 ATOM 4726 N VAL 650 58.046 16.755 -11.075 1.00 44.21 ATOM 4727 CA VAL 650 58.714 15.616 -11.696 1.00 48.14 ATOM 4728 CB VAL 650 58.401 15.483 -13.180 1.00 45.37 ATOM 4729 CG1 VAL 650 59.150 14.313 -13.731 1.00 47.12 ATOM 4730 CG2 VAL 650 56.923 15.311 -13.407 1.00 44.38 ATOM 4731 C VAL 650 60.196 15.817 -11.595 1.00 54.89 ATOM 4732 O VAL 650 60.766 16.662 -12.294 1.00 56.42 ATOM 4733 N GLN 651 60.817 15.043 -10.718 1.00 62.10 ATOM 4734 CA GLN 651 62.253 15.136 -10.510 1.00 71.53 ATOM 4735 CB GLN 651 62.568 15.175 -9.013 1.00 74.84 ATOM 4736 CG GLN 651 61.980 16.384 -8.294 1.00 80.23 ATOM 4737 CD GLN 651 62.380 16.453 -6.828 1.00 86.44 ATOM 4738 OE1 GLN 651 61.827 17.251 -6.065 1.00 88.07 ATOM 4739 NE2 GLN 651 63.341 15.616 -6.420 1.00 88.91 ATOM 4740 C GLN 651 62.978 13.981 -11.185 1.00 75.09 ATOM 4741 O GLN 651 63.591 13.140 -10.517 1.00 76.97 ATOM 4742 N LEU 652 62.892 13.966 -12.513 1.00 78.20 ATOM 4743 CA LEU 652 63.505 12.943 -13.354 1.00 80.82 ATOM 4744 CB LEU 652 63.468 13.404 -14.811 1.00 83.43 ATOM 4745 CG LEU 652 62.069 13.518 -15.418 1.00 84.78 ATOM 4746 CD1 LEU 652 62.119 14.172 -16.798 1.00 86.36 ATOM 4747 CD2 LEU 652 61.447 12.120 -15.483 1.00 85.69 ATOM 4748 C LEU 652 64.942 12.620 -12.960 1.00 82.59 ATOM 4749 OT1 LEU 652 65.216 11.449 -12.608 1.00 84.20 ATOM 4750 OT2 LEU 652 65.772 13.555 -13.013 1.00 86.03 ATOM 4751 O HOH 1 39.600 24.576 11.813 1.00 12.17 ATOM 4752 O HOH 2 40.792 27.069 11.597 1.00 25.65 ATOM 4753 O HOH 3 43.758 26.829 11.570 1.00 13.86 ATOM 4754 O HOH 4 55.446 23.281 8.689 1.00 39.72 ATOM 4755 O HOH 5 54.367 13.815 2.943 1.00 30.80 ATOM 4756 O HOH 6 57.911 14.284 16.519 1.00 30.98 ATOM 4757 O HOH 7 38.642 1.242 15.206 1.00 35.24 ATOM 4758 O HOH 8 39.462 -1.232 13.462 1.00 39.99 ATOM 4759 O HOH 9 30.581 9.208 17.185 1.00 12.58 ATOM 4760 O HOH 10 43.871 15.044 17.131 1.00 13.07 ATOM 4761 O HOH 11 57.356 -3.646 2.453 1.00 47.02 ATOM 4762 O HOH 12 45.059 -5.877 8.478 1.00 34.13 ATOM 4763 O HOH 13 42.458 6.455 1.498 1.00 37.54 ATOM 4764 O HOH 14 38.876 8.797 -1.848 1.00 29.14 ATOM 4765 O HOH 15 29.008 5.736 8.141 1.00 33.53 ATOM 4766 O HOH 16 26.319 10.581 4.483 0.50 34.39 ATOM 4767 O HOH 17 28.858 9.435 5.261 1.00 27.54 ATOM 4768 O HOH 18 30.989 23.542 6.740 1.00 27.62 ATOM 4769 O HOH 19 29.511 28.588 9.501 1.00 33.81 ATOM 4770 O HOH 20 45.641 8.025 6.242 1.00 20.04 ATOM 4771 O HOH 21 57.722 6.464 1.525 1.00 54.78 ATOM 4772 O HOH 22 48.699 27.494 1.748 1.00 30.06 ATOM 4773 O HOH 23 22.565 23.551 4.174 1.00 50.71 ATOM 4774 O HOH 24 31.780 26.111 1.799 1.00 36.59 ATOM 4775 O HOH 25 35.833 19.538 5.174 1.00 22.44 ATOM 4776 O HOH 26 31.698 41.144 14.808 1.00 26.75 ATOM 4777 O HOH 27 22.848 21.286 -7.106 0.50 44.55 ATOM 4778 O HOH 28 28.149 35.263 -5.749 0.50 27.52 ATOM 4779 O HOH 29 38.768 38.465 1.897 1.00 23.59 ATOM 4780 O HOH 30 36.036 48.871 -3.323 1.00 37.96 ATOM 4781 O HOH 31 15.228 54.291 25.146 1.00 38.59 ATOM 4782 O HOH 32 30.188 40.575 -3.853 1.00 25.30 ATOM 4783 O HOH 33 41.541 42.499 -1.499 1.00 33.25 ATOM 4784 O HOH 34 38.585 45.910 14.986 1.00 46.67 ATOM 4785 O HOH 35 39.850 41.334 2.080 1.00 44.36 ATOM 4786 O HOH 36 42.846 31.690 -10.923 1.00 21.98 ATOM 4787 O HOH 37 43.450 12.688 -1.919 1.00 24.87 ATOM 4788 O HOH 38 39.038 13.837 2.118 1.00 27.10 ATOM 4789 O HOH 39 37.928 5.313 -6.284 1.00 50.72 ATOM 4790 O HOH 40 24.875 4.116 -12.560 0.50 29.43 ATOM 4791 O HOH 41 55.553 35.810 -18.611 0.50 42.33 ATOM 4792 O HOH 42 46.764 34.401 3.319 1.00 52.37 ATOM 4793 O HOH 43 38.723 6.598 -19.519 1.00 45.34 ATOM 4794 O HOH 44 65.474 2.330 6.882 0.50 53.47 ATOM 4795 O HOH 45 62.312 4.587 26.852 0.50 32.00 ATOM 4796 O HOH 46 71.750 -5.969 18.706 1.00 37.47 ATOM 4797 O HOH 47 58.775 1.057 6.153 1.00 30.94 ATOM 4798 O HOH 48 45.175 6.998 1.494 1.00 34.82 ATOM 4799 O HOH 49 63.008 22.148 -6.426 0.50 29.98 ATOM 4800 O HOH 50 41.462 18.172 -0.139 1.00 30.33 ATOM 4801 O HOH 51 32.560 21.73 2.331 1.00 29.61 ATOM 4802 O HOH 52 14.519 37.667 0.321 0.50 37.60 ATOM 4803 O HOH 53 42.144 26.546 23.602 1.00 41.27 ATOM 4804 O HOH 54 54.172 23.431 6.327 1.00 37.79 ATOM 4805 O HOH 55 58.450 21.703 4.673 1.00 52.24 ATOM 4806 O HOH 56 53.956 13.326 12.026 1.00 49.78 ATOM 4807 O HOH 57 44.302 20.733 35.040 0.50 36.95 ATOM 4808 O HOH 58 25.387 22.349 29.206 1.00 51.45 ATOM 4809 O HOH 59 34.276 5.690 35.854 1.00 57.79 ATOM 4810 O HOH 60 32.551 5.395 26.460 1.00 44.81 ATOM 4811 O HOH 61 68.914 9.067 22.100 1.00 30.57 ATOM 4812 O HOH 62 69.607 4.862 7.019 1.00 68.86 ATOM 4813 O HOH 63 49.122 -5.437 19.972 0.50 32.90 ATOM 4814 O HOH 64 35.071 2.983 13.525 1.00 57.51 ATOM 4815 O HOH 65 69.205 -0.072 8.173 0.50 30.67 ATOM 4816 O HOH 66 59.499 -8.456 0.875 1.00 42.81 ATOM 4817 O HOH 67 43.513 -7.338 4.202 1.00 58.46 ATOM 4818 O HOH 68 24.836 23.892 5.544 1.00 25.95 ATOM 4819 O HOH 69 12.711 29.928 21.875 1.00 59.62 ATOM 4820 O HOH 70 11.349 34.141 13.154 1.00 37.81 ATOM 4821 O HOH 71 24.776 30.568 19.682 1.00 32.79 ATOM 4822 O HOH 72 35.674 22.015 5.914 1.00 25.68 ATOM 4823 O HOH 73 39.992 22.649 0.839 1.00 26.71 ATOM 4824 O HOH 74 33.304 19.359 1.262 1.00 21.88 ATOM 4825 O HOH 75 34.676 25.968 -1.544 1.00 25.47 ATOM 4826 O HOH 76 38.335 29.492 3.495 1.00 26.33 ATOM 4827 O HOH 77 34.285 32.668 -0.876 1.00 32.85 ATOM 4828 O HOH 78 26.762 34.664 2.474 1.00 38.71 ATOM 4829 O HOH 79 26.382 37.981 -5.606 1.00 42.31 ATOM 4830 O HOH 80 14.711 48.855 -4.418 0.50 35.57 ATOM 4831 O HOH 81 48.032 50.318 1.569 1.00 49.00 ATOM 4832 O HOH 82 40.081 36.290 12.462 1.00 18.52 ATOM 4833 O HOH 83 48.045 27.052 -4.303 1.00 33.60 ATOM 4834 O HOH 84 55.768 32.124 -2.269 0.50 25.70 ATOM 4835 O HOH 85 58.944 26.970 -4.766 1.00 33.86 ATOM 4836 O HOH 86 29.248 24.775 -22.246 1.00 25.41 ATOM 4837 O HOH 87 26.155 13.359 -0.686 1.00 50.23 ATOM 4838 O HOH 88 28.166 13.371 2.556 1.00 53.78 ATOM 4839 O HOH 89 31.879 55.238 18.930 0.50 45.82 ATOM 4840 O HOH 90 32.757 29.484 16.842 1.00 30.62 ATOM 4841 O HOH 91 34.578 30.002 24.337 0.50 45.60 ATOM 4842 O HOH 92 66.362 10.141 11.805 1.00 55.07 ATOM 4843 O HOH 93 65.292 7.242 12.256 1.00 30.58 ATOM 4844 O HOH 94 56.297 13.563 14.593 1.00 24.51 ATOM 4845 O HOH 95 45.123 21.767 30.085 1.00 49.84 ATOM 4846 O HOH 96 67.321 6.836 9.353 1.00 42.45 ATOM 4847 O HOH 97 51.532 37.990 -11.584 0.50 33.54 ATOM 4848 O HOH 98 34.637 24.900 25.435 0.50 36.72 ATOM 4849 O HOH 99 47.745 21.275 29.129 1.00 50.32 ATOM 4850 O HOH 100 29.797 24.486 22.331 1.00 29.64 ATOM 4851 O HOH 101 22.812 10.827 33.352 0.50 23.42 ATOM 4852 O HOH 102 30.142 2.352 26.582 1.00 58.88 ATOM 4853 O HOH 103 42.498 2.698 29.895 1.00 33.97 ATOM 4854 O HOH 104 45.548 1.707 29.609 1.00 35.08 ATOM 4855 O HOH 105 73.449 -5.044 16.464 1.00 48.73 ATOM 4856 O HOH 106 51.401 5.777 4.853 1.00 37.62 ATOM 4857 O HOH 107 59.811 -3.998 4.731 1.00 49.23 ATOM 4858 O HOH 108 23.913 36.019 17.692 1.00 51.86 ATOM 4859 O HOH 109 15.955 40.383 5.523 1.00 57.03 ATOM 4860 O HOH 110 24.683 23.216 -3.359 1.00 47.03 ATOM 4861 O HOH 111 27.878 49.199 -5.908 0.50 37.58 ATOM 4862 O HOH 112 40.089 51.139 -3.822 0.50 28.49 ATOM 4863 O HOH 113 1.194 48.031 17.761 0.50 31.30 ATOM 4864 O HOH 114 15.911 47.963 -1.509 0.50 41.57 ATOM 4865 O HOH 115 15.594 57.329 9.243 0.50 35.83 ATOM 4866 O HOH 116 18.349 44.617 -4.211 0.50 25.42 ATOM 4867 O HOH 117 33.773 56.268 5.129 1.00 50.98 ATOM 4868 O HOH 118 42.261 50.708 2.854 0.50 23.17 ATOM 4869 O HOH 119 31.149 49.232 23.790 1.00 48.45 ATOM 4870 O HOH 120 47.467 26.554 -0.478 1.00 35.12 ATOM 4871 O HOH 121 20.282 27.249 1.269 0.50 25.52 ATOM 4872 O HOH 122 17.915 27.001 0.130 0.50 43.66 ATOM 4873 O HOH 123 64.315 18.441 -9.136 0.50 50.91 ATOM 4874 O HOH 124 51.346 15.323 -23.558 1.00 49.83 ATOM 4875 O HOH 125 20.796 11.150 -11.607 0.50 30.99 ATOM 4876 O HOH 126 52.824 44.504 12.282 0.50 32.83 ATOM 4877 O HOH 127 53.398 41.694 12.905 1.00 48.52 ATOM 4878 O HOH 128 20.223 5.133 20.272 0.50 29.69 ATOM 4879 O HOH 129 27.206 1.320 21.447 1.00 27.19 ATOM 4880 O HOH 130 24.082 11.809 20.686 1.00 40.93 ATOM 4881 O HOH 131 23.900 10.267 17.824 1.00 50.50 ATOM 4882 O HOH 132 28.117 5.220 10.701 0.50 25.36 ATOM 4883 O HOH 133 31.375 10.930 3.919 1.00 33.16 ATOM 4884 O HOH 134 43.293 29.293 19.633 1.00 26.02 ATOM 4885 O HOH 135 47.906 33.111 9.169 1.00 37.21 ATOM 4886 O HOH 136 52.105 14.532 4.067 1.00 12.30 ATOM 4887 O HOH 137 59.327 14.609 8.309 1.00 27.43 ATOM 4888 O HOH 138 61.489 16.241 7.756 1.00 36.45 ATOM 4889 O HOH 139 59.814 12.113 -0.094 1.00 41.19 ATOM 4890 O HOH 140 61.602 19.322 14.212 1.00 39.66 ATOM 4891 O HOH 141 44.822 14.088 27.205 1.00 43.44 ATOM 4892 O HOH 142 32.324 15.005 22.197 1.00 37.81 ATOM 4893 O HOH 143 23.735 25.109 18.876 1.00 34.70 ATOM 4894 O HOH 144 47.464 8.852 31.617 1.00 42.97 ATOM 4895 O HOH 145 63.649 6.056 25.352 1.00 24.23 ATOM 4896 O HOH 146 57.557 -8.767 13.297 1.00 54.16 ATOM 4897 O HOH 147 65.381 -8.112 17.380 1.00 53.12 ATOM 4898 O HOH 148 54.869 -3.233 3.058 1.00 20.55 ATOM 4899 O HOH 149 50.284 2.436 7.783 1.00 21.77 ATOM 4900 O HOH 150 40.450 4.556 1.629 1.00 36.03 ATOM 4901 O HOH 151 38.315 4.435 -0.621 1.00 54.82 ATOM 4902 O HOH 152 39.033 12.192 4.575 1.00 23.18 ATOM 4903 O HOH 153 20.487 17.422 16.380 1.00 42.43 ATOM 4904 O HOH 154 7.330 29.380 14.617 1.00 59.85 ATOM 4905 O HOH 155 11.575 29.095 8.037 1.00 27.89 ATOM 4906 O HOH 156 60.466 18.094 -3.688 1.00 39.21 ATOM 4907 O HOH 157 34.227 30.218 -0.200 1.00 16.99 ATOM 4908 O HOH 158 29.064 33.844 1.330 1.00 39.62 ATOM 4909 O HOH 159 27.587 37.46 5.225 1.00 26.48 ATOM 4910 O HOH 160 37.792 35.558 1.617 1.00 40.88 ATOM 4911 O HOH 161 22.032 47.398 12.372 1.00 29.56 ATOM 4912 O HOH 162 17.084 42.773 3.217 1.00 59.52 ATOM 4913 O HOH 163 38.184 53.069 2.626 1.00 37.51 ATOM 4914 O HOH 164 33.711 48.526 17.994 1.00 58.73 ATOM 4915 O HOH 165 32.371 44.192 22.263 0.50 33.76 ATOM 4916 O HOH 166 37.657 54.587 9.034 0.50 31.48 ATOM 4917 O HOH 167 27.552 46.211 26.991 1.00 61.96 ATOM 4918 O HOH 168 32.011 38.955 21.518 1.00 25.08 ATOM 4919 O HOH 169 47.499 35.638 18.696 1.00 35.40 ATOM 4920 O HOH 170 28.459 38.533 12.567 1.00 51.70 ATOM 4921 O HOH 171 53.929 21.580 -6.399 1.00 24.95 ATOM 4922 O HOH 172 26.651 18.234 -2.713 0.50 33.29 ATOM 4923 O HOH 173 42.655 15.443 -1.278 1.00 30.29 ATOM 4924 O HOH 174 45.560 26.974 -24.441 0.50 26.40 ATOM 4925 O HOH 175 52.934 29.907 -19.523 0.50 32.71 ATOM 4926 O HOH 176 26.381 16.979 -21.475 1.00 55.80 ATOM 4927 O HOH 177 46.523 8.953 -25.135 1.00 55.70 ATOM 4928 O HOH 178 41.397 7.159 -12.350 1.00 49.45 ATOM 4929 O HOH 179 37.051 1.869 -16.152 0.50 22.12 ATOM 4930 O HOH 180 48.915 13.423 -22.645 0.50 38.37 ATOM 4931 O HOH 181 51.414 33.545 -13.567 1.00 27.21 ATOM 4932 O HOH 182 40.136 20.409 14.870 1.00 50.68 ATOM 4933 O HOH 183 27.368 20.586 29.572 0.50 22.75 ATOM 4934 O HOH 184 33.144 15.340 33.325 0.50 34.27 ATOM 4935 O HOH 185 41.866 10.270 32.855 0.50 27.94 ATOM 4936 O HOH 186 36.169 7.373 38.507 0.50 28.46 ATOM 4937 O HOH 187 65.230 13.163 12.508 0.50 29.96 ATOM 4938 O HOH 188 69.243 -3.143 14.989 0.50 21.97 ATOM 4939 O HOH 189 70.109 8.508 12.586 0.50 40.05 ATOM 4940 O HOH 190 68.136 1.192 12.530 1.00 30.68 ATOM 4941 O HOH 191 46.519 -1.841 24.920 1.00 51.89 ATOM 4942 O HOH 192 35.512 0.276 23.742 1.00 58.13 ATOM 4943 O HOH 193 27.272 4.449 13.576 1.00 41.45 ATOM 4944 O HOH 194 20.663 4.047 27.178 0.50 42.21 ATOM 4945 O HOH 195 62.540 2.570 8.192 1.00 35.49 ATOM 4946 O HOH 196 56.134 -12.022 8.682 1.00 51.96 ATOM 4947 O HOH 197 51.156 -5.845 11.368 1.00 38.51 ATOM 4948 O HOH 198 47.936 -5.942 12.718 1.00 46.17 ATOM 4949 O HOH 199 46.547 -7.383 10.304 1.00 42.53 ATOM 4950 O HOH 200 31.686 4.036 10.011 0.50 39.93 ATOM 4951 O HOH 201 18.345 18.429 18.069 1.00 52.41 ATOM 4952 O HOH 202 8.319 32.684 12.203 1.00 58.05 ATOM 4953 O HOH 203 30.148 26.964 7.489 0.50 17.11 ATOM 4954 O HOH 204 30.520 29.659 18.757 1.00 41.82 ATOM 4955 O HOH 205 41.389 15.889 1.196 1.00 41.86 ATOM 4956 O HOH 206 59.747 12.116 -2.964 1.00 42.54 ATOM 4957 O HOH 207 59.220 20.606 1.293 0.50 33.12 ATOM 4958 O HOH 208 45.462 27.614 -3.993 1.00 53.13 ATOM 4959 O HOH 209 8.977 42.303 22.785 0.50 28.98 ATOM 4960 O HOH 210 7.375 36.792 15.794 0.50 25.08 ATOM 4961 O HOH 211 20.262 31.233 -0.791 0.50 23.07 ATOM 4962 O HOH 212 22.775 37.068 -1.456 0.50 26.21 ATOM 4963 O HOH 213 31.515 33.290 -8.299 1.00 39.56 ATOM 4964 O HOH 214 32.528 28.894 -2.045 0.50 30.57 ATOM 4965 O HOH 215 23.556 52.964 -3.369 0.50 37.73 ATOM 4966 O HOH 216 12.291 55.849 23.454 1.00 31.77 ATOM 4967 O HOH 217 24.234 62.724 15.579 1.00 62.11 ATOM 4968 O HOH 218 16.102 49.162 8.905 1.00 25.74 ATOM 4969 O HOH 219 28.120 39.039 -4.114 1.00 29.56 ATOM 4970 O HOH 220 44.251 45.804 -12.595 0.50 34.94 ATOM 4971 O HOH 221 29.607 44.784 -10.015 1.00 60.29 ATOM 4972 O HOH 222 25.270 58.721 8.796 1.00 53.22 ATOM 4973 O HOH 223 34.170 56.320 7.918 1.00 50.34 ATOM 4974 O HOH 224 35.135 51.082 -1.204 0.50 45.57 ATOM 4975 O HOH 225 45.412 41.610 0.691 0.50 25.74 ATOM 4976 O HOH 226 46.994 48.580 6.406 1.00 47.90 ATOM 4977 O HOH 227 27.014 55.791 16.344 1.00 33.70 ATOM 4978 O HOH 228 20.619 63.647 20.163 0.50 25.46 ATOM 4979 O HOH 229 27.098 63.600 13.977 1.00 52.38 ATOM 4980 O HOH 230 29.921 62.241 15.115 0.50 31.33 ATOM 4981 O HOH 231 39.209 34.131 21.722 1.00 44.63 ATOM 4982 O HOH 232 27.446 37.346 19.046 1.00 53.39 ATOM 4983 O HOH 233 41.629 34.505 14.339 1.00 49.50 ATOM 4984 O HOH 234 49.929 25.940 20.363 0.50 65.78 ATOM 4985 O HOH 235 46.595 25.050 21.969 1.00 60.97 ATOM 4986 O HOH 236 45.546 28.752 21.088 1.00 60.57 ATOM 4987 O HOH 237 11.993 48.397 8.380 1.00 50.42 ATOM 4988 O HOH 238 47.384 34.817 0.402 1.00 45.46 ATOM 4989 O HOH 239 24.707 20.747 3.321 0.50 36.30 ATOM 4990 O HOH 240 24.997 27.004 0.759 0.50 31.67 ATOM 4991 O HOH 241 35.294 20.250 -2.672 1.00 55.67 ATOM 4992 O HOH 242 25.636 12.744 -6.207 0.50 34.82 ATOM 4993 O HOH 243 50.790 14.313 -15.411 1.00 40.65 ATOM 4994 O HOH 244 60.682 29.709 -18.658 1.00 63.57 ATOM 4995 O HOH 245 55.814 30.382 -22.340 0.50 42.64 ATOM 4996 O HOH 246 35.354 4.428 -6.477 1.00 37.57 ATOM 4997 O HOH 247 28.238 6.114 -2.367 1.00 50.71 ATOM 4998 O HOH 248 55.861 14.928 -21.178 1.00 56.34 ATOM 4999 O HOH 249 59.791 24.221 -18.460 1.00 49.24 ATOM 5000 O HOH 250 28.695 10.159 -21.579 1.00 57.39 ATOM 5001 O HOH 251 23.322 9.183 -18.681 0.50 36.90 END 8.2 CRYSTAL COORDINATES OF CRY3A HEADER TOXIN 22-JUN-941DLC 1DLC 2 COMPND DELTA-ENDOTOXIN CRYIIIA (BT13)1DLC 3 SOURCE (BACILLUS THURINGIENSIS, SUBSPECIES TENEBRIONIS)1DLC 4 AUTHORJ. LI 1DLC 5 REVDAT 1 30-SEP-941DLC 01DLC 6 REMARK 1 1DLC 7REMARK 1REFERENCE 1 1DLC 8REMARK 1 AUTH J. LI, J. CARROLL, D. J. ELLAR1DLC 9REMARK 1 TITL CRYSTAL STRUCTURE OF INSECTICIDAL DELTA-ENDOTOXIN1DLC 10REMARK 1TITL 2 FROM BACILLUS THURINGIENSIS AT 2.5 ANGSTROMS1DLC 11REMARK 1TITL 3RESOLUTION 1DLC 12REMARK 1 REF NATURE V. 353 815 19911DLC 13REMARK 1 REFN ASTM NATUAS UK ISSN 0028-0836 00061DLC 14REMARK 1REFERENCE 21DLC 15REMARK 1 AUTH J. LI, R. HENDERSON, J. CARROLL, D. ELLAR1DLC 16REMARK 1 TITL X-RAY ANALYSIS OF THE CRYSTALLINE PARASPORAL1DLC 17 REMARK 1TITL 2 INCLUSION IN BACILLUS THURINGIENSIS VAR.1DLC 18REMARK 1TITL 3 TENEBRIONIS1DLC 19REMARK 1 REF J. MOL. BIOL. V. 199 543 19881DLC 20REMARK 1 REFN ASTM JMOBAK UK ISSN 0022-2836 00701DLC 21 REMARK 2 1DLC 22REMARK 2 RESOLUTION. 2.5 ANGSTROMS.1DLC 23 REMARK 31DLC 24REMARK 3 REFINEMENT.1DLC 25REMARK 3PROGRAM X-PLOR 1DLC 26 REMARK 3 AUTHORS BRUNGER1DLC 27 REMARK 3 R VALUE 0.1831DLC 28REMARK 3 RMSD BOND DISTANCES 0.011 ANGSTROMS1DLC 29 REMARK 3 RMSD BOND ANGLES 1.58 DEGREES1DLC 30REMARK 3 RMSD DIHEDRAL ANGLES 25.06 DEGREES1DLC 31REMARK 3 RMSD IMPROPER ROTATION 1.471 DEGREES1DLC 32 REMARK 31DLC 33REMARK 3 NUMBER OF REFLECTIONS 277261DLC 34REMARK 3 RESOLUTION RANGE 16.0-2.5 ANGSTROMS1DLC 35 REMARK 3 DATA CUTOFF 0.0 SIGMA(F) 1DLC 36 REMARK 3 PERCENT COMPLETION 100.1DLC 37 REMARK 31DLC 38REMARK 3 NUMBER OF PROTEIN ATOMS 46971DLC 39REMARK 3 NUMBER OF SOLVENT ATOMS 1061DLC 40 REMARK 3 1DLC 41REMARK 3 THE ATOMIC MODEL INCLUDES RESIDUES 61-644 OF THE1DLC 42REMARK 3 AND 106 BOUND WATER MOLECULES. BULKSOLVENT CONTRIBUTION 1DLC 43REMARK 3 TO THE STRUCTURE FACTOR WAS CALCULATED USING THE 1DLC 44REMARK 3 PROGRAM SFALL AND INCLUDED IN THIS REFINEMENT. 1DLC 45 REMARK 3 1DLC 46 REMARK 4 1DLC 47REMARK 4 CRYIIIA BELONGS TO THE "1CRY" FAMILY OF DELTA-ENDOTOXINS,1DLC 48REMARK 4 WHICH ARE PORE-FORMING INSECTICIDAL PROTEIN TOXINS1DLC 49REMARK 4 CONTAINED IN THE CRYSTALLINEPARASPORAL INCLUSIONS 1DLC 50REMARK 4 BACILLUS THURINGIENSIS. THE SUBCLASS III ISTOXIC 1DLC 51REMARK 4 SPECIFICALLY TO COLEOPTERAN INSECTS, I.E., BEETLES.1DLC 52REMARK 4 FUNCTION BY BINDING TO MIDGUT EPITHELIAL CELLS AND1DLC 53REMARK 4 COLLOIDOSMOTIC LYSIS.1DLC 54 REMARK 5 1DLC SS REMARK 5 THE SEQUENCE OF CRYIIIA IN THE ATOMIC MODEL IS TAKEN1DLC 56REMARK 5 HOEFTE, H., SEURINCK, J., VAN HOUTVEN, A. AND VAECK, 1DLC 57 REMARK 5 (1987) NUCLEIC ACIDS RES. 15:7183. EMBL ACCESSION 1DLC 58 REMARK 5 P07130, ENTRY NAME CR70.sub.-- BACTT. RESIDUES 1-571DLC 59REMARK 5 REMOVED IN THE MATURE TOXIN. RESIDUES 58-60 ARE1DLC 60REMARK 5 INVISIBLE IN THE CRYSTAL STRUCTURE. 1DLC 61 REMARK 6 1DLC 62REMARK 6 THE STRUCTURE WAS REPORTED IN PAPER [1] ABOVE AFTER 1DLC 63REMARK 6 PRELIMIMARY REFINEMENT. THE COORDINATES BEING DEPOSITED 1DLC 64REMARK 6 HERE RESULTED FROM FURTHER REFINEMENT. 1DLC 65 REMARK 7 1DLC 66 REMARK 7 CROSS REFERENCE TO SEQUENCE DATABASE 1DLC 67 REMARK 7 SWISS-PROT ENTRY NAME PDB ENTRY CHAIN NAME 1DLC 68 REMARK 7 CR70.sub.-- BACTT 1DLC 69SEQRES 1 584 THR THR LYS ASP VAL ILE GLN LYS GLY ILE SER VAL VAL 1DLC 70SEQRES 2 584 GLY ASP LEU LEU GLY VAL VAL GLY PHE PRO PHE GLY GLY 1DLC 71SEQRES 3 584 ALA LEU VAL SER PHE TYR THR ASN PHE LEU ASN THR ILE 1DLC 72SEQRES 4 584 TRP PRO SER GLU ASP PRO TRP LYS ALA PHE MET GLU GLN 1DLC 73 SEQRES 5 584 VAL GLU ALA LEU MET ASP GLN LYS ILE ALA ASP TYR ALA 1DLC 74 SEQRES 6 584 LYS ASN LYS ALA LEU ALA GLU LEU GLN GLY LEU GLN ASN 1DLC 75 SEQRES 7 584 ASN VAL GLU ASP TYR VAL SER ALA LEU SER SER TRP GLN 1DLC 76 SEQRES 8 584 LYS ASN PRO VAL SER SER ARG ASN PRO HIS SER GLN GLY 1DLC 77 SEQRES 9 584 ARG ILE ARG GLU LEU PHE SER GLN ALA GLU SER HIS PHE 1DLC 78 SEQRES 10 584 ARG ASN SER MET PRO SER PHE ALA ILE SER GLY TYR GLU 1DLC 79 SEQRES 11 584 VAL LEU PHE LEU THR THR TYR ALA GLN ALA ALA ASN THR 1DLC 80 SEQRES 12 584 HIS LEU PHE LEU LEU LYS ASP ALA GLN ILE TYR GLY GLU 1DLC 81SEQRES 13 584 GLU TRP GLY TYR GLU LYS GLU ASP ILE ALA GLU PHE TYR 1DLC 82SEQRES 14 584 LYS ARG GLN LEU LYS LEU THR GLN GLU TYR THR ASP HIS 1DLC 83SEQRES 15 584 CYS VAL LYS TRP TYR ASN VAL GLY LEU ASP LYS LEU ARG 1DLC 84 SEQRES 16 584 GLY SER SER TYR GLU SER TRP VAL ASN PHE ASN ARG TYR 1DLC 85 SEQRES 17 584 ARG ARG GLU MET THR LEU THR VAL LEU ASP LEU ILE ALA 1DLC 86 SEQRES 18 584 LEU PHE PRO LEU TYR ASP VAL ARG LEU TYR PRD LYS GLU 1DLC 87 SEQRES 19 584 VAL LYS THR GLU LEU THR ARG ASP VAL LEU THR ASP PRO 1DLC 88 SEQRES 20 584 ILE VAL GLY VAL ASN ASN LEU ARG GLY TYR GLY THR THR 1DLC 89 SEQRES 21 584 PHE SER ASN ILE GLU ASN TYR ILE ARG LYS PRO HIS LEU 1DLC 90 SEQRES 22 584 PHE ASP TYR LEU HIS ARG ILE GLN PHE HIS THR ARG PHE 1DLC 91 SEQRES 23 584 GLN PRO GLY TYR TYR GLY ASN ASP SER PHE ASN TYR TRP 1DLC 92SEQRES 24 584 SER GLY ASN TYR VAL SER THR ARG PRO SER ILE GLY SER 1DLC 93 SEQRES 25 584 ASN ASP ILE ILE THR SER PRO PHE TYR GLY ASN LYS SER 1DLC 94 SEQRES 26 584 SER GLU PRO VAL GLN ASN LEU GLU PHE ASN GLY GLU LYS 1DLC 95 SEQRES 27 584 VAL TYR ARG ALA VAL ALA ASN THR ASN LEU ALA VAL TRP 1DLC 96 SEQRES 28 584 PRO SER ALA VAL TYR SER GLY VAL THR LYS VAL GLU PHE 1DLC 97 SEQRES 29 584 SER GLN TYR ASN ASP GLN THR ASP GLU ALA SER THR GLN 1DLC 98 SEQRES 30 584 THR TYR ASP SER LYS ARG ASN VAL GLY ALA VAL SER TRP 1DLC 99 SEQRES 31 584 ASP SER ILE ASP GLN LEU PRO PRO GLU THR THR ASP GLU 1DLC 100 SEQRES 32 584 PRO LEU GLU LYS GLY TYR SER HIS GLN LEU ASN TYR VAL 1DLC 101 SEQRES 33 584 MET CYS PHE LEU MET GLN GLY SER ARG GLY THR ILE PRO 1DLC 102SEQRES 34 584 VAL LEU THR TRP THR HIS LYS SER VAL ASP PHE PHE ASN 1DLC 103 SEQRES 35 584 MET ILE ASP SER LYS LYS ILE THR GLN LEU PRO LEU VAL 1DLC 104SEQRES 36 584 LYS ALA TYR LYS LEU GLN SER GLY ALA SER VAL VAL ALA 1DLC 105SEQRES 37 584 GLY PRO ARG PHE THR GLY GLY ASP ILE ILE GLN CYS THR 1DLC 106SEQRES 38 584 GLU ASN GLY SER ALA ALA THR ILE TYR VAL THR PRO ASP 1DLC 107 SEQRES 39 584 VAL SER TYR SER GLN LYS TYR ARG ALA ARG ILE HIS TYR 1DLC 108SEQRES 40 584 ALA SER THR SER GLN ILE THR PHE THR LEU SER LEU ASP 1DLC 109 SEQRES 41 584 GLY ALA PRO PHE ASN GLN TYR TYR PHE ASP LYS THR ILE 1DLC 110 SEQRES 42 584 ASN LYS GLY ASP THR LEU THR TYR ASN SER PHE ASN LEU 1DLC 111 SEQRES 43 584 ALA SER PHE SER THR PRO PHE GLU LEU SER GLY ASN ASN 1DLC 112 SEQRES 44 584 LEU GLN ILE GLY VAL THR GLY LEU SER ALA GLY ASP LYS 1DLC 113 SEQRES 45 584 VAL TYR ILE ASP LYS ILE GLU PHE ILE PRO VAL ASN 1DLC 114 FTNOTE 1 1DLC 115FTNOTE 1 RESIDUE ARG 443 IS MODELED IN TWO CONFORMATIONS. 1DLC 116FORMUL 2 HOH *106(H2 O1) 1DLC 117 CRYST1 117.090 134.260 104.500 90.00 90.00 90.00C 2 2 21 8 1DLC 118 ORIGX1 1.000000 0.000000 0.000000 0.00000 1DLC 119 ORIGX2 0.000000 1.000000 0.000000 0.00000 1DLC 120 ORIGX3 0.000000 0.000000 1.000000 0.00000 1DLC 121 SCALE1 0.008540 0.000000 0.000000 0.00000 1DLC 122 SCALE2 0.000000 0.007448 0.000000 0.00000 1DLC 123 SCALE3 0.000000 0.000000 0.009569 0.00000 1DLC 124 ATOM 1 N THR 61 29.687 34.216 28.976 1.00 81.05 1DLC 125 ATOM 2 CA THR 61 29.891 35.382 28.051 1.00 79.92 1DLC 126 ATOM 3 C THR 61 30.511 36.562 28.809 1.00 78.01 1DLC 127 ATOM 4 O THR 61 30.542 36.553 30.039 1.00 78.99 1DLC 128 ATOM 5 CB THR 61 28.566 35.808 27.359 1.00 81.30 1DLC 129 ATOM 6 OG1 THR 61 28.815 36.906 26.470 1.00 81.70 1DLC 130 ATOM 7 CG2 THR 61 27.514 36.206 28.388 1.00 82.00 1DLC 131 ATOM 8 N THR 62 31.035 37.542 28.074 1.00 74.62 1DLC 132 ATOM 9 CA THR 62 31.689 38.735 28.648 1.00 71.74 1DLC 133 ATOM 10 C THR 62 32.886 38.447 29.565 1.00 68.69 1DLC 134 ATOM 11 O THR 62 33.402 39.348 30.227 1.00 67.78 1DLC 135 ATOM 12 CB THR 62 30.702 39.676 29.416 1.00 72.26 1DLC 136 ATOM 13 OG1 THR 62 30.353 39.108 30.689 1.00 70.81 1DLC 137 ATOM 14 CG2 THR 62 29.446 39.935 28.595 1.00 72.45 1DLC 138 ATOM 15 N LYS 63 33.367 37.206 29.542 1.00 65.97 1DLC 139 ATOM 16 CA LYS 63 34.505 36.792 30.369 1.00 64.35 1DLC 140 ATOM 17 C LYS 63 35.716 37.704 30.142 1.00 60.39 1DLC 141 ATOM 18 O LYS 63 36.514 37.928 31.050 1.00 58.79 1DLC 142 ATOM 19 CB LYS 63 34.903 35.327 30.097 1.00 67.19 1DLC 143 ATOM 20 CG LYS 63 33.799 34.413 29.553 1.00 71.54 1DLC 144 ATOM 21 CD LYS 63 33.671 34.566 28.032 1.00 77.47 1DLC 145 ATOM 22 CE LYS 63 32.583 33.671 27.434 1.00 79.28 1DLC 146 ATOM 23 NZ LYS 63 32.253 34.062 26.018 1.00 79.70 1DLC 147 ATOM 24 N ASP 64 35.829 38.242 28.928 1.00 56.53 1DLC 148 ATOM 25 CA ASP 64 36.919 39.146 28.568 1.00 52.15 1DLC 149 ATOM 26 C ASP 64 37.009 40.333 29.526 1.00 46.41 1DLC 150 ATOM 27 O ASP 64 38.033 40.514 30.176 1.00 45.73 1DLC 151 ATOM 28 CB ASP 64 36.747 39.647 27.131 1.00 59.48 1DLC 152 ATOM 29 CG ASP 64 37.811 40.666 26.729 1.00 66.90 1DLC 153 ATOM 30 OD1 ASP 64 39.020 40.354 26.864 1.00 70.25 1DLC 154 ATOM 31 OD2 ASP 64 37.436 41.780 26.280 1.00 70.28 1DLC 155 ATOM 32 N VAL 65 35.937 41.120 29.631 1.00 40.49 1DLC 156 ATOM 33 CA VAL 65 35.929 42.276 30.535 1.00 36.43 1DLC 157 ATOM 34 C VAL 65 35.981 41.865 31.998 1.00 33.19 1DLC 158 ATOM 35 O VAL 65 36.481 42.612 32.843 1.00 33.95 1DLC 159 ATOM 36 CB VAL 65 34.721 43.233 30.319 1.00 34.54 1DLC 160 ATOM 37 CG1 VAL 65 34.823 43.903 28.969 1.00 35.83 1DLC 161 ATOM 38 CG2 VAL 65 33.405 42.501 30.473 1.00 36.36 1DLC 162 ATOM 39 N ILE 66 35.474 40.676 32.299 1.00 28.34 1DLC 163 ATOM 40 CA ILE 66 35.506 40.187 33.666 1.00 26.84 1DLC 164 ATOM 41 C ILE 66 36.953 39.854 34.029 1.00 27.43 1DLC 165 ATOM 42 O ILE 66 37.405 40.153 35.138 1.00 27.70 1DLC 166 ATOM 43 CB ILE 66 34.576 38.962 33.857 1.00 26.34 1DLC 167 ATOM 44 CG1 ILE 66 33.138 39.362 33.533 1.00 26.70 1DLC 168 ATOM 45 CG2 ILE 66 34.627 38.459 35.299 1.00 23.41 1DLC 169 ATOM 46 CD1 ILE 66 32.625 40.529 34.377 1.00 27.75 1DLC 170 ATOM 47 N GLN 67 37.696 39.313 33.063 1.00 26.53 1DLC 171 ATOM 48 CA GLN 67 39.100 38.962 33.278 1.00 27.75 1DLC 172 ATOM 49 C GLN 67 39.931 40.231 33.442 1.00 25.84 1DLC 173 ATOM 50 O GLN 67 40.772 40.315 34.340 1.00 23.91 1DLC 174 ATOM 51 CB GLN 67 39.639 38.122 32.122 1.00 32.89 1DLC 175 ATOM 52 CG GLN 67 40.360 36.852 32.576 1.00 39.52 1DLC 176 ATOM 53 CD GLN 67 41.866 37.006 32.729 1.00 44.36 1DLC 177 ATOM 54 OE1 GLN 67 42.613 36.080 32.442 1.00 52.02 1DLC 178 ATOM 55 NE2 GLN 67 42.316 38.156 33.188 1.00 45.86 1DLC 179 ATOM 56 N LYS 68 39.688 41.216 32.580 1.00 22.97 1DLC 180 ATOM 57 CA LYS 68 40.388 42.496 32.664 1.00 24.69 1DLC 181 ATOM 58 C LYS 68 40.100 43.123 34.030 1.00 24.93 1DLC 182 ATOM 59 O LYS 68 41.010 43.577 34.725 1.00 28.51 1DLC 183 ATOM 60 CB LYS 68 39.926 43.436 31.550 1.00 26.181DLC 184 ATOM 61 CG LYS 68 40.265 42.946 30.158 1.00 29.43 1DLC 185 ATOM 62 CD LYS 68 39.812 43.936 29.098 1.00 35.76 1DLC 186 ATOM 63 CE LYS 68 40.187 43.453 27.710 1.00 37.351DLC 187 ATOM 64 NZ LYS 68 41.635 43.087 27.651 1.00 43.99 1DLC 188 ATOM 65 N GLY 69 38.832 43.092 34.431 1.00 24.56 1DLC 189 ATOM 66 CA GLY 69 38.443 43.632 35.717 1.00 22.62 1DLC 190 ATOM 67 C GLY 69 39.161 42.937 36.859 1.00 22.361DLC 191 ATOM 68 O GLY 69 39.750 43.599 37.709 1.00 25.641DLC 192 ATOM 69 N ILE 70 39.144 41.606 36.862 1.00 20.461DLC 193 ATOM 70 CA ILE 70 39.801 40.821 37.908 1.00 19.461DLC 194 ATOM 71 C ILE 70 41.318 41.037 37.943 1.00 21.56 1DLC 195 ATOM 72 O ILE 70 41.911 41.211 39.015 1.00 20.57 1DLC 196 ATOM 73 CB ILE 70 39.452 39.303 37.773 1.00 21.33 1DLC 197 ATOM 74 CG1 ILE 70 37.984 39.074 38.191 1.00 21.901DLC 198 ATOM 75 CG2 ILE 70 40.413 38.437 38.609 1.00 17.07 1DLC 199 ATOM 76 CD1 ILE 70 37.517 37.621 38.227 1.00 15.87 1DLC 200 ATOM 77 N SER 71 41.929 41.072 36.763 1.00 22.901DLC 201 ATOM 78 CA SER 71 43.371 41.277 36.627 1.00 24.321DLC 202 ATOM 79 C SER 71 43.861 42.628 37.141 1.00 23.60 1DLC 203 ATOM 80 O SER 71 44.873 42.697 37.845 1.00 23.301DLC 204 ATOM 81 CB SER 71 43.795 41.111 35.171 1.00 25.61 1DLC 205 ATOM 82 OG SER 71 43.497 39.802 34.733 1.00 34.05 1DLC 206 ATOM 83 N VAL 72 43.153 43.698 36.787 1.00 20.94 1DLC 207 ATOM 84 CA VAL 72 43.532 45.037 37.232 1.00 20.83 1DLC 208 ATOM 85 C VAL 72 43.556 45.113 38.755 1.00 21.24 1DLC 209 ATOM 86 O VAL 72 44.528 45.584 39.346 1.00 23.21 1DLC 210 ATOM 87 CB VAL 72 42.572 46.104 36.673 1.00 22.69 1DLC 211 ATOM 88 CG1 VAL 72 42.850 47.458 37.309 1.00 24.49 1DLC 212 ATOM 89 CG2 VAL 72 42.738 46.203 35.165 1.00 25.89 1DLC 213 ATOM 90 N VAL 73 42.493 44.613 39.380 1.00 19.28 1DLC 214 ATOM 91 CA VAL 73 42.377 44.600 40.834 1.00 15.95 1DLC 215 ATOM 92 C VAL 73 43.523 43.777 41.408 1.00 15.90 1DLC 216 ATOM 93 O VAL 73 44.169 44.181 42.373 1.00 19.54 1DLC 217 ATOM 94 CB VAL 73 40.993 44.023 41.277 1.00 15.19 1DLC 218 ATOM 95 CG1 VAL 73 40.977 43.726 42.762 1.00 11.40 1DLC 219 ATOM 96 CG2 VAL 73 39.882 45.005 40.936 1.00 8.14 1DLC 220 ATOM 97 N GLY 74 43.804 42.643 40.773 1.00 18.80 1DLC 221 ATOM 98 CA GLY 74 44.888 41.786 41.225 1.00 20.25 1DLC 222 ATOM 99 C GLY 74 46.250 42.465 41.136 1.00 22.94 1DLC 223 ATOM 100 O GLY 74 47.061 42.353 42.051 1.00 24.08 1DLC 224 ATOM 101 N ASP 75 46.493 43.183 40.043 1.00 21.18 1DLC 225 ATOM 102 CA ASP 75 47.750 43.892 39.849 1.00 25.01 1DLC 226 ATOM 103 C ASP 75 47.858 45.070 40.810 1.00 25.78 1DLC 227 ATOM 104 O ASP 75 48.904 45.296 41.423 1.00 27.64 1DLC 228 ATOM 105 CB ASP 75 47.873 44.394 38.404 1.00 31.86 1DLC 229 ATOM 106 CG ASP 75 48.091 43.263 37.397 1.00 35.66 1DLC 230 ATOM 107 OD1 ASP 75 48.511 42.153 37.802 1.00 39.68 1DLC 231 ATOM 108 OD2 ASP 75 47.847 43.487 36.189 1.00 42.21 1DLC 232 ATOM 109 N LEU 76 46.772 45.819 40.947 1.00 26.59 1DLC 233 ATOM 110 CA LEU 76 46.755 46.967 41.847 1.00 24.97 1DLC 234 ATOM 111 C LEU 76 47.065 46.549 43.276 1.00 23.34 1DLC 235 ATOM 112 O LEU 76 47.690 47.303 44.018 1.00 23.84 1DLC 236 ATOM 113 CB LEU 76 45.410 47.678 41.790 1.00 24.54 1DLC 237 ATOM 114 CG LEU 76 45.214 48.589 40.588 1.00 21.89 1DLC 238 ATOM 115 CD1 LEU 76 43.743 48.951 40.475 1.00 23.58 1DLC 239 ATOM 116 CD2 LEU 76 46.081 49.830 40.737 1.00 20.301DLC 240 ATOM 117 N LEU 77 46.655 45.339 43.649 1.00 22.54 1DLC 241 ATOM 118 CA LEU 77 46.928 44.834 44.992 1.00 23.75 1DLC 242 ATOM 119 C LEU 77 48.440 44.786 45.278 1.00 24.55 1DLC 243 ATOM 120 O LEU 77 48.864 44.713 46.435 1.00 25.25 1DLC 244 ATOM 121 CB LEU 77 46.290 43.453 45.198 1.00 22.14 1DLC 245 ATOM 122 CG LEU 77 44.817 43.440 45.633 1.00 23.83 1DLC 246 ATOM 123 CD1 LEU 77 44.298 42.016 45.692 1.00 21.52 1DLC 247 ATOM 124 CD2 LEU 77 44.652 44.116 46.991 1.00 19.85 1DLC 248 ATOM 125 N GLY 78 49.240 44.837 44.215 1.00 24.11 1DLC 249 ATOM 126 CA GLY 78 50.684 44.823 44.356 1.00 23.63 1DLC 250 ATOM 127 C GLY 78 51.337 46.203 44.380 1.00 25.07 1DLC 251 ATOM 128 O GLY 78 52.481 46.329 44.795 1.00 28.69 1DLC 252 ATOM 129 N VAL 79 50.634 47.238 43.930 1.00 24.83 1DLC 253 ATOM 130 CA VAL 79 51.190 48.599 43.920 1.00 22.91 1DLC 254 ATOM 131 C VAL 79 50.332 49.576 44.728 1.00 23.48 1DLC 255 ATOM 132 O VAL 79 50.285 50.775 44.461 1.00 28.13 1DLC 256 ATOM 133 CB VAL 79 51.361 49.136 42.474 1.00 19.52 1DLC 257 ATOM 134 CG1 VAL 79 52.454 48.379 41.769 1.00 19.64 1DLC 258 ATOM 135 CG2 VAL 79 50.072 49.007 41.701 1.00 18.98 1DLC 259 ATOM 136 N VAL 80 49.666 49.047 45.736 1.00 23.04 1DLC 260 ATOM 137 CA VAL 80 48.795 49.835 46.588 1.00 21.33 1DLC 261 ATOM 138 C VAL 80 49.632 50.446 47.753 1.00 24.09 1DLC 262 ATOM 139 O VAL 80 50.565 49.810 48.267 1.00 24.41 1DLC 263 ATOM 140 CB VAL 80 47.575 48.936 46.982 1.00 16.03 1DLC 264 ATOM 141 CG1 VAL 80 47.581 48.546 48.431 1.00 16.04 1DLC 265 ATOM 142 CG2 VAL 80 46.295 49.576 46.531 1.00 8.70 1DLC 266 ATOM 143 N GLY 81 49.345 51.694 48.123 1.00 23.56 1DLC 267 ATOM 144 CA GLY 81 50.134 52.364 49.150 1.00 20.79 1DLC 268 ATOM 145 C GLY 81 51.281 53.059 48.416 1.00 24.82 1DLC 269 ATOM 146 O GLY 81 51.128 53.400 47.244 1.00 26.66 1DLC 270 ATOM 147 N PHE 82 52.419 53.292 49.067 1.00 26.10 1DLC 271 ATOM 148 CA PHE 82 53.567 53.934 48.401 1.00 24.09 1DLC 272 ATOM 149 C PHE 82 54.383 52.816 47.747 1.00 24.46 1DLC 273 ATOM 150 O PHE 82 55.143 52.114 48.425 1.00 26.54 1DLC 274 ATOM 151 CB PHE 82 54.429 54.684 49.417 1.00 22.55 1DLC 275 ATOM 152 CG PHE 82 55.329 55.721 48.808 1.00 27.94 1DLC 276 ATOM 153 CD1 PHE 82 56.374 55.359 47.963 1.00 31.41 1DLC 277 ATOM 154 CD2 PHE 82 55.136 57.069 49.080 1.00 30.52 1DLC 278 ATOM 155 CE1 PHE 82 57.215 56.327 47.395 1.00 31.44 1DLC 279 ATOM 156 CE2 PHE 82 55.972 58.048 48.518 1.00 31.81 1DLC 280 ATOM 157 CZ PHE 82 57.012 57.673 47.674 1.00 30.74 1DLC 281 ATOM 158 N PRO 83 54.278 52.671 46.412 1.00 23.78 1DLC 282 ATOM 159 CA PRO 83 54.988 51.632 45.663 1.00 26.68 1DLC 283 ATOM 160 C PRO 83 56.418 51.983 45.255 1.00 30.99 1DLC 284 ATOM 161 O PRO 83 56.763 53.156 45.095 1.00 31.60 1DLC 285 ATOM 162 CB PRO 83 54.107 51.475 44.430 1.00 23.32 1DLC 286 ATOM 163 CG PRO 83 53.801 52.905 44.103 1.00 24.30 1DLC 287 ATOM 164 CD PRO 83 53.578 53.578 45.481 1.00 24.78 1DLC 288 ATOM 165 N PHE 84 57.248 50.962 45.054 1.00 35.72 1DLC 289 ATOM 166 CA PHE 84 58.610 51.222 44.622 1.00 37.68 1DLC 290 ATOM 167 C PHE 84 58.622 51.455 43.101 1.00 36.16 1DLC 291 ATOM 168 O PHE 84 57.928 50.768 42.344 1.00 35.44 1DLC 292 ATOM 169 CB PHE 84 59.585 50.142 45.149 1.00 43.35 1DLC 293 ATOM 170 CG PHE 84 60.018 49.109 44.139 1.00 53.50 1DLC 294 ATOM 171 CD1 PHE 84 60.836 49.450 43.055 1.00 55.35 1DLC 295 ATOM 172 CD2 PHE 84 59.682 47.768 44.324 1.00 58.10 1DLC 296 ATOM 173 CE1 PHE 84 61.311 48.473 42.178 1.00 57.42 1DLC 297 ATOM 174 CE2 PHE 84 60.156 46.778 43.448 1.00 59.43 1DLC 298 ATOM 175 CZ PHE 84 60.971 47.133 42.375 1.00 58.66 1DLC 299 ATOM 176 N GLY 85 59.320 52.515 42.701 1.00 34.26 1DLC 300 ATOM 177 CA GLY 85 59.427 52.923 41.308 1.00 31.90 1DLC 301 ATOM 178 C GLY 85 59.414 51.874 40.213 1.00 31.82 1DLC 302 ATOM 179 O GLY 85 58.751 52.062 39.193 1.00 33.93 1DLC 303 ATOM 180 N GLY 86 60.183 50.803 40.385 1.00 30.52 1DLC 304 ATOM 181 CA GLY 86 60.205 49.750 39.380 1.00 30.25 1DLC 305 ATOM 182 C GLY 86 58.868 49.035 39.291 1.00 29.35 1DLC 306 ATOM 183 O GLY 86 58.369 48.752 38.204 1.00 29.94 1DLC 307 ATOM 184 N ALA 87 58.273 48.764 40.445 1.00 27.51 1DLC 308 ATOM 185 CA ALA 87 56.980 48.103 40.492 1.00 26.98 1DLC 309 ATOM 186 C ALA 87 55.905 48.972 39.833 1.00 27.22 1DLC 310 ATOM 187 O ALA 87 55.085 48.473 39.064 1.00 31.29 1DLC 311 ATOM 188 CB ALA 87 56.606 47.796 41.927 1.00 28.74 1DLC 312 ATOM 189 N LEU 88 55.944 50.276 40.106 1.00 26.83 1DLC 313 ATOM 190 CA LEU 88 54.982 51.239 39.551 1.00 25.69 1DLC 314 ATOM 191 C LEU 88 55.005 51.264 38.018 1.00 27.21 1DLC 315 ATOM 192 O LEU 88 53.955 51.221 37.364 1.00 27.87 1DLC 316 ATOM 193 CB LEU 88 55.274 52.637 40.110 1.00 27.08 1DLC 317 ATOM 194 CG LEU 88 54.208 53.744 40.185 1.00 27.37 1DLC 318 ATOM 195 CD1 LEU 88 54.504 54.862 39.217 1.00 24.51 1DLC 319 ATOM 196 CD2 LEU 88 52.817 53.179 39.972 1.00 30.411DLC 320 ATOM 197 N VAL 89 56.207 51.308 37.448 1.00 28.98 1DLC 321 ATOM 198 CA VAL 89 56.369 51.325 35.993 1.00 28.90 1DLC 322 ATOM 199 C VAL 89 55.898 50.001 35.387 1.00 29.01 1DLC 323 ATOM 200 O VAL 89 55.165 49.999 34.396 1.00 28.22 1DLC 324 ATOM 201 CB VAL 89 57.828 51.644 35.594 1.00 27.87 1DLC 325 ATOM 202 CG1 VAL 89 57.975 51.678 34.082 1.00 24.97 1DLC 326 ATOM 203 CG2 VAL 89 58.222 52.996 36.169 1.00 28.04 1DLC 327 ATOM 204 N SER 90 56.278 48.885 36.013 1.00 30.42 1DLC 328 ATOM 205 CA SER 90 55.856 47.551 35.559 1.00 32.29 1DLC 329 ATOM 206 C SER 90 54.342 47.506 35.485 1.00 32.55 1DLC 330 ATOM 207 O SER 90 53.765 47.085 34.479 1.00 34.09 1DLC 331 ATOM 208 CB SER 90 56.295 46.472 36.544 1.00 34.34 1DLC 332 ATOM 209 OG SER 90 57.694 46.292 36.525 1.00 46.73 1DLC 333 ATOM 210 N PHE 91 53.701 47.924 36.575 1.00 31.31 1DLC 334 ATOM 211 CA PHE 91 52.249 47.956 36.633 1.00 29.77 1DLC 335 ATOM 212 C PHE 91 51.712 48.737 35.441 1.00 29.48 1DLC 336 ATOM 213 O PHE 91 50.912 48.224 34.668 1.00 31.29 1DLC 337 ATOM 214 CB PHE 91 51.758 48.622 37.924 1.00 29.25 1DLC 338 ATOM 215 CG PHE 91 50.285 48.926 37.911 1.00 27.24 1DLC 339 ATOM 216 CD1 PHE 91 49.354 47.923 38.151 1.00 24.90 1DLC 340 ATOM 217 CD2 PHE 91 49.828 50.197 37.584 1.00 24.88 1DLC 341 ATOM 218 CE1 PHE 91 47.996 48.176 38.057 1.00 24.42 1DLC 342 ATOM 219 CE2 PHE 91 48.469 50.458 37.489 1.00 23.79 1DLC 343 ATOM 220 CZ PHE 91 47.554 49.446 37.724 1.00 22.85 1DLC 344 ATOM 221 N TYR 92 52.176 49.972 35.294 1.00 29.52 1DLC 345 ATOM 222 CA TYR 92 51.736 50.835 34.211 1.00 29.00 1DLC 346 ATOM 223 C TYR 92 51.764 50.214 32.815 1.00 30.26 1DLC 347 ATOM 224 O TYR 92 50.858 50.466 32.017 1.00 30.35 1DLC 348 ATOM 225 CB TYR 92 52.524 52.141 34.222 1.00 29.47 1DLC 349 ATOM 226 CG TYR 92 51.925 53.227 35.088 1.00 27.60 1DLC 350 ATOM 227 CD1 TYR 92 50.587 53.603 34.947 1.00 27.51 1DLC 351 ATOM 228 CD2 TYR 92 52.716 53.938 35.993 1.00 24.64 1DLC 352 ATOM 229 CE1 TYR 92 50.062 54.669 35.677 1.00 25.83 1DLC 353 ATOM 230 CE2 TYR 92 52.197 54.999 36.726 1.00 21.65 1DLC 354 ATOM 231 CZ TYR 92 50.876 55.363 36.562 1.00 23.23 1DLC 355 ATOM 232 OH TYR 92 50.380 56.440 37.260 1.00 21.02 1DLC 356 ATOM 233 N THR 93 52.774 49.396 32.515 1.00 30.64 1DLC 357 ATOM 234 CA THR 93 52.839 48.771 31.190 1.00 32.20 1DLC 358 ATOM 235 C THR 93 51.743 47.724 31.004 1.00 33.10 1DLC 359 ATOM 236 O THR 93 51.126 47.658 29.945 1.00 34.96 1DLC 360 ATOM 237 CB THR 93 54.226 48.171 30.866 1.00 33.29 1DLC 361 ATOM 238 OG1 THR 93 54.487 47.041 31.704 1.00 39.40 1DLC 362 ATOM 239 CG2 THR 93 55.308 49.213 31.080 1.00 34.17 1DLC 363 ATOM 240 N ASN 94 51.479 46.926 32.038 1.00 33.43 1DLC 364 ATOM 241 CA ASN 94 50.406 45.929 31.965 1.00 36.98 1DLC 365 ATOM 242 C ASN 94 49.089 46.685 31.856 1.00 35.78 1DLC 366 ATOM 243 O ASN 94 48.244 46.375 31.018 1.00 37.99 1DLC 367 ATOM 244 CB ASN 94 50.348 45.068 33.230 1.00 44.19 1DLC 368 ATOM 245 CG ASN 94 51.398 43.978 33.253 1.00 51.52 1DLC 369 ATOM 246 OD1 ASN 94 52.109 43.753 32.272 1.00 54.17 1DLC 370 ATOM 247 ND2 ASN 94 51.490 43.277 34.381 1.00 54.88 1DLC 371 ATOM 248 N PHE 95 48.942 47.692 32.713 1.00 33.93 1DLC 372 ATOM 249 CA PHE 95 47.755 48.538 32.771 1.00 33.38 1DLC 373 ATOM 250 C PHE 95 47.398 49.047 31.385 1.00 32.29 1DLC 374 ATOM 251 O PHE 95 46.270 48.895 30.927 1.00 34.55 1DLC 375 ATOM 252 CB PHE 95 48.017 49.715 33.713 1.00 33.16 1DLC 376 ATOM 253 CG PHE 95 46.806 50.551 34.005 1.00 32.63 1DLC 377 ATOM 254 CD1 PHE 95 45.602 49.953 34.386 1.00 30.05 1DLC 378 ATOM 255 CD2 PHE 95 46.873 51.941 33.920 1.00 31.23 1DLC 379 ATOM 256 CE1 PHE 95 44.485 50.726 34.678 1.00 29.10 1DLC 380 ATOM 257 CE2 PHE 95 45.761 52.726 34.210 1.00 28.92 1DLC 381 ATOM 258 CZ PHE 95 44.566 52.117 34.590 1.00 31.14 1DLC 382 ATOM 259 N LEU 96 48.380 49.614 30.702 1.00 34.97 1DLC 383 ATOM 260 CA LEU 96 48.166 50.126 29.360 1.00 35.92 1DLC 384 ATOM 261 C LEU 96 47.771 49.028 28.384 1.00 36.69 1DLC 385 ATOM 262 O LEU 96 46.903 49.230 27.539 1.00 39.72 1DLC 386 ATOM 263 CB LEU 96 49.409 50.869 28.862 1.00 39.72 1DLC 387 ATOM 264 CG LEU 96 49.427 52.393 29.075 1.00 42.79 1DLC 388 ATOM 265 CD1 LEU 96 49.134 52.771 30.537 1.00 43.39 1DLC 389 ATOM 266 CD2 LEU 96 50.776 52.937 28.633 1.00 45.04 1DLC 390 ATOM 267 N ASN 97 48.371 47.853 28.523 1.00 37.06 1DLC 391 ATOM 268 CA ASN 97 48.050 46.738 27.630 1.00 40.47 1DLC 392 ATOM 269 C ASN 97 46.665 46.150 27.893 1.00 39.49 1DLC 393 ATOM 270 O ASN 97 45.986 45.680 26.981 1.00 41.34 1DLC 394 ATOM 271 CB ASN 97 49.103 45.629 27.741 1.00 49.91 1DLC 395 ATOM 272 CG ASN 97 50.459 46.054 27.219 1.00 42.87 1DLC 396 ATOM 273 OD1 ASN 97 51.489 45.589 27.699 1.00 47.11 1DLC 397 ATOM 274 ND2 ASN 97 50.469 46.941 26.234 1.00 38.77 1DLC 398 ATOM 275 N THR 98 46.244 46.214 29.144 1.00 38.36 1DLC 399 ATOM 276 CA THR 98 44.959 45.677 29.543 1.00 36.23 1DLC 400 ATOM 277 C THR 98 43.798 46.638 29.306 1.00 33.62 1DLC 401 ATOM 278 O THR 98 42.957 46.412 28.445 1.00 34.42 1DLC 402 ATOM 279 CB THR 98 44.983 45.290 31.039 1.00 37.03 1DLC 403 ATOM 280 OG1 THR 98 46.134 44.479 31.302 1.00 36.69 1DLC 404 ATOM 281 CG2 THR 98 43.726 44.516 31.427 1.00 39.60 1DLC 405 ATOM 282 N ILE 99 43.796 47.740 30.045 1.00 31.37 1DLC 406 ATOM 283 CA ILE 99 42.720 48.722 29.983 1.00 28.14 1DLC 407 ATOM 284 C ILE 99 42.837 49.822 28.923 1.00 30.20 1DLC 408 ATOM 285 O ILE 99 41.827 50.244 28.351 1.00 30.60 1DLC 409 ATOM 286 CB ILE 99 42.523 49.378 31.383 1.00 25.44 1DLC 410 ATOM 287 CG1 ILE 99 42.274 48.301 32.445 1.00 23.31 1DLC 411 ATOM 288 CG2 ILE 99 41.389 50.388 31.362 1.00 24.47 1DLC 412 ATOM 289 CD1 ILE 99 41.002 47.504 32.253 1.00 24.55 1DLC 413 ATOM 290 N TRP 100 44.056 50.270 28.631 1.00 29.78 1DLC 414 ATOM 291 CA TRP 100 44.226 51.355 27.661 1.00 30.90 1DLC 415 ATOM 292 C TRP 100 44.913 51.060 26.312 1.00 34.13 1DLC 416 ATOM 293 O TRP 100 45.593 51.932 25.755 1.00 37.64 1DLC 417 ATOM 294 CB TRP 100 44.916 52.548 28.341 1.00 25.25 1DLC 418 ATOM 295 CG TRP 100 44.160 53.138 29.509 1.00 21.47 1DLC 419 ATOM 296 CD1 TRP 100 44.326 52.835 30.836 1.00 19.22 1DLC 420 ATOM 297 CD2 TRP 100 43.173 54.181 29.459 1.00 19.56 1DLC 421 ATOM 298 NE1 TRP 100 43.517 53.635 31.611 1.00 19.74 1DLC 422 ATOM 299 CE2 TRP 100 42.799 54.469 30.795 1.00 19.03 1DLC 423 ATOM 300 CE3 TRP 100 42.576 54.905 28.418 1.00 16.14 1DLC 424 ATOM 301 CZ2 TRP 100 41.856 55.455 31.116 1.00 20.11 1DLC 425 ATOM 302 CZ3 TRP 100 41.635 55.887 28.739 1.00 18.05 1DLC 426 ATOM 303 CH2 TRP 100 41.287 56.150 30.079 1.00 18.97 1DLC 427 ATOM 304 N PRO 101 44.702 49.859 25.738 1.00 35.80 1DLC 428 ATOM 305 CA PRO 101 45.347 49.557 24.455 1.00 37.30 1DLC 429 ATOM 306 C PRO 101 44.651 50.132 23.217 1.00 38.37 1DLC 430 ATOM 307 O PRO 101 45.309 50.557 22.271 1.00 39.64 1DLC 431 ATOM 308 CB PRO 101 45.322 48.034 24.431 1.00 38.85 1DLC 432 ATOM 309 CG PRO 101 44.017 47.726 25.088 1.00 35.28 1DLC 433 ATOM 310 CD PRO 101 44.032 48.658 26.274 1.00 36.12 1DLC 434 ATOM 311 N SER 102 43.322 50.129 23.227 1.00 40.19 1DLC 435 ATOM 312 CA SER 102 42.514 50.620 22.105 1.00 41.68 1DLC 436 ATOM 313 C SER 102 41.097 50.916 22.592 1.00 41.86 1DLC 437 ATOM 314 O SER 102 40.831 50.852 23.789 1.00 41.66 1DLC 438 ATOM 315 CB SER 102 42.439 49.547 21.019 1.00 43.16 1DLC 439 ATOM 316 OG SER 102 41.925 48.330 21.556 1.00 45.57 1DLC 440 ATOM 317 N GLU 103 40.178 51.206 21.674 1.00 41.50 1DLC 441 ATOM 318 CA GLU 103 38.800 51.482 22.080 1.00 43.73 1DLC 442 ATOM 319 C GLU 103 37.989 50.207 22.334 1.00 41.43 1DLC 443 ATOM 320 O GLU 103 36.916 50.251 22.937 1.00 40.77 1DLC 444 ATOM 321 CB GLU 103 38.078 52.403 21.076 1.00 48.24 1DLC 445 ATOM 322 CG GLU 103 37.564 51.764 19.782 1.00 56.59 1DLC 446 ATOM 323 CD GLU 103 38.656 51.448 18.766 1.00 63.51 1DLC 447 ATOM 324 OE1 GLU 103 39.739 52.096 18.786 1.00 66.38 1DLC 448 ATOM 325 OE2 GLU 103 38.417 50.544 17.931 1.00 65.54 1DLC 449 ATOM 326 N ASP 104 38.544 49.065 21.947 1.00 40.07 1DLC 450 ATOM 327 CA ASP 104 37.856 47.791 22.132 1.00 41.15 1DLC 451 ATOM 328 C ASP 104 37.437 47.481 23.572 1.00 38.99 1DLC 452 ATOM 329 O ASP 104 36.282 47.118 23.816 1.00 39.97 1DLC 453 ATOM 330 CB ASP 104 38.674 46.634 21.543 1.00 44.04 1DLC 454 ATOM 331 CG ASP 104 38.713 46.656 20.016 1.00 50.06 1DLC 455 ATOM 332 OD1 ASP 104 37.649 46.852 19.375 1.00 53.14 1DLC 456 ATOM 333 OD2 ASP 104 39.811 46.468 19.454 1.00 53.68 1DLC 457 ATOM 334 N PRO 105 38.351 47.651 24.551 1.00 36.35 1DLC 458 ATOM 335 CA PRO 105 37.984 47.364 25.944 1.00 34.16 1DLC 459 ATOM 336 C PRO 105 36.845 48.263 26.449 1.00 33.17 1DLC 460 ATOM 337 O PRO 105 35.899 47.794 27.089 1.00 31.65 1DLC 461 ATOM 338 CB PRO 105 39.286 47.640 26.703 1.00 32.33 1DLC 462 ATOM 339 CG PRO 105 40.336 47.374 25.695 1.00 32.70 1DLC 463 ATOM 340 CD PRO 105 39.773 48.023 24.464 1.00 33.69 1DLC 464 ATOM 341 N TRP 106 36.933 49.548 26.127 1.00 30.91 1DLC 465 ATOM 342 CA TRP 106 35.928 50.519 26.543 1.00 31.51 1DLC 466 ATOM 343 C TRP 106 34.573 50.226 25.925 1.00 30.83 1DLC 467 ATOM 344 O TRP 106 33.539 50.353 26.572 1.00 31.34 1DLC 468 ATOM 345 CB TRP 106 36.404 51.928 26.200 1.00 30.77 1DLC 469 ATOM 346 CG TRP 106 37.688 52.230 26.890 1.00 31.17 1DLC 470 ATOM 347 CD1 TRP 106 38.940 52.165 26.356 1.00 28.87 1DLC 471 ATOM 348 CD2 TRP 106 37.858 52.537 28.277 1.00 31.01 1DLC 472 ATOM 349 NE1 TRP 106 39.879 52.396 27.327 1.00 27.96 1DLC 473 ATOM 350 CE2 TRP 106 39.245 52.629 28.517 1.00 29.45 1DLC 474 ATOM 351 CE3 TRP 106 36.971 52.737 29.346 1.00 32.12 1DLC 475 ATOM 352 CZ2 TRP 106 39.771 52.912 29.781 1.00 31.59 1DLC 476 ATOM 353 CZ3 TRP 106 37.495 53.019 30.607 1.00 33.16 1DLC 477 ATOM 354 CH2 TRP 106 38.884 53.103 30.811 1.00 31.59 1DLC 478 ATOM 355 N LYS 107 34.588 49.786 24.678 1.00 33.17 1DLC 479 ATOM 356 CA LYS 107 33.356 49.445 23.979 1.00 35.51 1DLC 480 ATOM 357 C LYS 107 32.718 48.208 24.638 1.00 31.75 1DLC 481 ATOM 358 O LYS 107 31.499 48.136 24.818 1.00 27.83 1DLC 482 ATOM 359 CB LYS 107 33.674 49.188 22.506 1.00 40.04 1DLC 483 ATOM 360 CG LYS 107 32.519 49.475 21.568 1.00 49.75 1DLC 484 ATOM 361 CD LYS 107 33.032 49.919 20.204 1.00 56.89 1DLC 485 ATOM 362 CE LYS 107 34.066 48.945 19.643 1.00 62.13 1DLC 486 ATOM 363 NZ LYS 107 34.425 49.301 18.238 1.00 68.80 1DLC 487 ATOM 364 N ALA 108 33.574 47.276 25.055 1.00 29.83 1DLC 488 ATOM 365 CA ALA 108 33.160 46.045 25.720 1.00 28.62 1DLC 489 ATOM 366 C ALA 108 32.569 46.312 27.115 1.00 29.18 1DLC 490 ATOM 367 O ALA 108 31.662 45.598 27.559 1.00 28.23 1DLC 491 ATOM 368 C ALA 108 34.344 45.083 25.810 1.00 27.06 1DLC 492 ATOM 369 N PHE 109 33.092 47.327 27.806 1.00 27.51 1DLC 493 ATOM 370 CA PHE 109 32.589 47.701 29.129 1.00 26.94 1DLC 494 ATOM 371 C PHE 109 31.193 48.301 29.013 1.00 27.69 1DLC 495 ATOM 372 O PHE 109 30.338 48.104 29.876 1.00 29.41 1DLC 496 ATOM 373 CB PHE 109 33.525 48.703 29.805 1.00 27.56 1DLC 497 ATOM 374 CG PHE 109 34.672 48.064 30.528 1.00 32.09 1DLC 498 ATOM 375 CD1 PHE 109 34.465 46.954 31.344 1.00 33.41 1DLC 499 ATOM 376 CD2 PHE 109 35.962 48.566 30.396 1.00 32.21 1DLC 500 ATOM 377 CE1 PHE 109 35.523 46.351 32.018 1.00 34.60 1DLC 501 ATOM 378 CE2 PHE 109 37.025 47.972 31.065 1.00 34.23 1DLC 502 ATOM 379 CZ PHE 109 36.805 46.860 31.879 1.00 34.84 1DLC 503 ATOM 380 N MET 110 30.970 49.047 27.942 1.00 26.88 1DLC 504 ATOM 381 CA MET 110 29.671 49.653 27.713 1.00 29.57 1DLC 505 ATOM 382 C MET 110 28.666 48.544 27.402 1.00 31.10 1DLC 506 ATOM 383 O MET 110 27.614 48.442 28.038 1.00 30.88 1DLC 507 ATOM 384 CB MET 110 29.751 50.664 26.564 1.00 29.18 1DLC 508 ATOM 385 CG MET 110 30.604 51.894 26.869 1.00 28.37 1DLC 509 ATOM 386 CD MET 110 30.715 53.039 25.473 1.00 32.631DLC 510 ATOM 387 CE MET 110 31.965 54.148 26.035 1.00 35.77 1DLC 511 ATOM 388 N GLU 111 29.033 47.672 26.467 1.00 33.04 1DLC 512 ATOM 389 CA GLU 111 28.179 46.553 26.078 1.00 33.48 1DLC 513 ATOM 390 C GLU 111 27.885 45.632 27.257 1.00 31.71 1DLC 514 ATOM 391 O GLU 111 26.801 45.054 27.338 1.00 30.92 1DLC 515 ATOM 392 CB GLU 111 28.818 45.755 24.937 1.00 37.35 1DLC 516 ATOM 393 CG GLU 111 28.863 46.510 23.607 1.00 45.28 1DLC 517 ATOM 394 CD GLU 111 29.578 45.753 22.491 1.00 48.00 1DLC 518 ATOM 395 OE1 GLU 111 29.969 44.577 22.690 1.00 52.24 1DLC 519 ATOM 396 OE2 GLU 111 29.755 46.350 21.407 1.00 49.92 1DLC 520 ATOM 397 N GLN 112 28.839 45.526 28.183 1.00 30.24 1DLC 521 ATOM 398 CA GLN 112 28.671 44.682 29.368 1.00 28.58 1DLC 522 ATOM 399 C GLN 112 27.431 45.058 30.182 1.00 28.06 1DLC 523 ATOM 400 O GLN 112 26.565 44.217 30.454 1.00 29.19 1DLC 524 ATOM 401 CB GLN 112 29.896 44.760 30.280 1.00 26.24 1DLC 525 ATOM 402 CG GLN 112 29.763 43.882 31.517 1.00 27.12 1DLC 526 ATOM 403 CD GLN 112 30.677 44.295 32.644 1.00 27.16 1DLC 527 ATOM 404 OE1 GLN 112 31.050 45.456 32.767 1.00 27.74 1DLC 528 ATOM 405 NE2 GLN 112 31.032 43.348 33.484 1.00 29.40 1DLC 529 ATOM 406 N VAL 113 27.337 46.325 30.560 1.00 24.97 1DLC 530 ATOM 407 CA VAL 113 26.201 46.764 31.349 1.00 23.68 1DLC 531 ATOM 408 C VAL 113 24.932 46.792 30.519 1.00 24.60 1DLC 532 ATOM 409 O VAL 113 23.853 46.539 31.031 1.00 27.38 1DLC 533 ATOM 410 CB VAL 113 26.462 48.114 32.003 1.00 20.75 1DLC 534 ATOM 411 CG1 VAL 113 25.401 48.398 33.048 1.00 16.74 1DLC 535 ATOM 412 CG2 VAL 113 27.846 48.106 32.642 1.00 21.83 1DLC 536 ATOM 413 N GLU 114 25.060 47.071 29.228 1.00 28.20 1DLC 537 ATOM 414 CA GLU 114 23.894 47.081 28.351 1.00 27.34 1DLC 538 ATOM 415 C GLU 114 23.268 45.681 28.368 1.00 27.33 1DLC 539 ATOM 416 O GLU 114 22.048 45.527 28.410 1.00 27.26 1DLC 540 ATOM 417 CB GLU 114 24.305 47.455 26.929 1.00 27.02 1DLC 541 ATOM 418 CG GLU 114 24.757 48.893 26.776 1.00 29.51 1DLC 542 ATOM 419 CD GLU 114 25.075 49.250 25.338 1.00 29.59 1DLC 543 ATOM 420 OE1 GLU 114 25.765 48.464 24.654 1.00 33.56 1DLC 544 ATOM 421 OE2 GLU 114 24.629 50.319 24.883 1.00 30.80 1DLC 545 ATOM 422 N ALA 115 24.128 44.667 28.384 1.00 25.38 1DLC 546 ATOM 423 CA ALA 115 23.700 43.276 28.425 1.00 23.38 1DLC 547 ATOM 424 C ALA 115 22.994 42.964 29.735 1.00 24.92 1DLC 548 ATOM 425 O ALA 115 21.939 42.357 29.731 1.00 30.01 1DLC 549 ATOM 426 CB ALA 115 24.892 42.357 28.248 1.00 23.08 1DLC 550 ATOM 427 N LEU 116 23.584 43.381 30.850 1.00 25.64 1DLC 551 ATOM 428 CA LEU 116 23.008 43.153 32.179 1.00 26.66 1DLC 552 ATOM 429 C LEU 116 21.688 43.895 32.397 1.00 27.99 1DLC 553 ATOM 430 O LEU 116 20.761 43.382 33.023 1.00 29.24 1DLC 554 ATOM 431 CB LEU 116 23.992 43.598 33.270 1.00 25.03 1DLC 555 ATOM 432 CG LEU 116 25.261 42.770 33.501 1.00 28.01 1DLC 556 ATOM 433 CD1 LEU 116 26.257 43.525 34.380 1.00 26.20 1DLC 557 ATOM 434 CD2 LEU 116 24.890 41.442 34.132 1.00 27.91 1DLC 558 ATOM 435 N MET 117 21.614 45.109 31.873 1.00 28.41 1DLC 559 ATOM 436 CA MET 117 20.442 45.957 32.032 1.00 30.17 1DLC 560 ATOM 437 C MET 117 19.390 45.825 30.934 1.00 31.82 1DLC 561 ATOM 438 O MET 117 18.252 46.256 31.102 1.00 31.84 1DLC 562 ATOM 439 CB MET 117 20.903 47.408 32.099 1.00 30.05 1DLC 563 ATOM 440 CG MET 117 20.528 48.129 33.361 1.00 31.75 1DLC 564 ATOM 441 SD MET 117 20.999 47.259 34.847 1.00 32.52 1DLC 565 ATOM 442 CE MET 117 19.682 47.817 35.885 1.00 24.44 1DLC 566 ATOM 443 N ASP 118 19.776 45.223 29.818 1.00 33.29 1DLC 567 ATOM 444 CA ASP 118 18.894 45.073 28.666 1.00 37.23 1DLC 568 ATOM 445 C ASP 118 18.412 46.445 28.203 1.00 37.19 1DLC 569 ATOM 446 O ASP 118 17.225 46.683 27.979 1.00 37.25 1DLC 570 ATOM 447 CB ASP 118 17.716 44.144 28.956 1.00 42.38 1DLC 571 ATOM 448 CG ASP 118 17.205 43.450 27.697 1.00 47.50 1DLC 572 ATOM 449 OD1 ASP 118 18.027 42.797 27.009 1.00 50.29 1DLC 573 ATOM 450 OD2 ASP 118 15.993 43.564 27.392 1.00 50.50 1DLC 574 ATOM 451 N GLN 119 19.372 47.355 28.106 1.00 39.11 1DLC 575 ATOM 452 CA GLN 119 19.151 48.722 27.660 1.00 39.37 1DLC 576 ATOM 453 C GLN 119 20.371 49.116 26.849 1.00 39.51 1DLC 577 ATOM 454 O GLN 119 21.416 48.478 26.946 1.00 41.09 1DLC 578 ATOM 455 CB GLN 119 19.029 49.674 28.841 1.00 41.10 1DLC 579 ATOM 456 CG GLN 119 17.784 49.520 29.657 1.00 47.05 1DLC 580 ATOM 457 CD GLN 119 17.628 50.660 30.637 1.00 52.24 1DLC 581 ATOM 458 OE1 GLN 119 17.745 50.484 31.851 1.00 54.31 1DLC 582 ATOM 459 NE2 GLN 119 17.385 51.850 30.111 1.00 55.17 1DLC 583 ATOM 460 N LYS 120 20.250 50.179 26.066 1.00 41.11 1DLC 584 ATOM 461 CA LYS 120 21.361 50.647 25.250 1.00 38.74 1DLC 585 ATOM 462 C LYS 120 21.613 52.129 25.433 1.00 38.08 1DLC 586 ATOM 463 O LYS 120 20.710 52.890 25.773 1.00 39.76 1DLC 587 ATOM 464 CB LYS 120 21.100 50.341 23.779 1.00 41.32 1DLC 588 ATOM 465 CG LYS 120 21.203 48.862 23.444 1.00 47.56 1DLC 589 ATOM 466 CD LYS 120 20.881 48.608 21.991 1.00 54.971DLC 590 ATOM 467 CE LYS 120 21.147 47.160 21.615 1.00 59.79 1DLC 591 ATOM 468 NZ LYS 120 20.761 46.901 20.190 1.00 67.72 1DLC 592 ATOM 469 N ILE 121 22.863 52.524 25.265 1.00 37.13 1DLC 593 ATOM 470 CA ILE 121 23.241 53.921 25.385 1.00 37.29 1DLC 594 ATOM 471 C ILE 121 22.939 54.602 24.039 1.00 38.92 1DLC 595 ATOM 472 O ILE 121 23.157 54.009 22.977 1.00 39.34 1DLC 596 ATOM 473 CB ILE 121 24.749 54.063 25.715 1.00 34.38 1DLC 597 ATOM 474 CG1 ILE 121 25.097 53.244 26.961 1.00 35.00 1DLC 598 ATOM 475 CG2 ILE 121 25.089 55.514 25.969 1.00 34.52 1DLC 599 ATOM 476 CD1 ILE 121 26.580 53.116 27.247 1.00 31.52 1DLC 600 ATOM 477 N ALA 122 22.383 55.811 24.081 1.00 37.83 1DLC 601 ATOM 478 CA ALA 122 22.083 56.545 22.854 1.00 37.13 1DLC 602 ATOM 479 C ALA 122 23.388 56.682 22.075 1.00 38.77 1DLC 603 ATOM 480 O ALA 122 24.391 57.131 22.629 1.00 42.15 1DLC 604 ATOM 481 CB ALA 122 21.528 57.909 23.189 1.00 31.82 1DLC 605 ATOM 482 N ASP 123 23.386 56.275 20.808 1.00 40.84 1DLC 606 ATOM 483 CA ASP 123 24.588 56.342 19.971 1.00 42.51 1DLC 607 ATOM 484 C ASP 123 25.452 57.587 20.115 1.00 40.46 1DLC 608 ATOM 485 O ASP 123 26.671 57.482 20.157 1.00 37.07 1DLC 609 ATOM 486 CB ASP 123 24.239 56.135 18.501 1.00 51.37 1DLC 610 ATOM 487 CG ASP 123 24.397 54.690 18.069 1.00 59.26 1DLC 611 ATOM 488 OD1 ASP 123 25.508 54.135 18.240 1.00 63.83 1DLC 612 ATOM 489 OD2 ASP 123 23.414 54.107 17.560 1.00 65.85 1DLC 613 ATOM 490 N TYR 124 24.821 58.756 20.210 1.00 41.62 1DLC 614 ATOM 491 CA TYR 124 25.554 60.015 20.361 1.00 41.32 1DLC 615 ATOM 492 C TYR 124 26.390 59.997 21.645 1.00 41.19 1DLC 616 ATOM 493 O TYR 124 27.575 60.341 21.633 1.00 44.09 1DLC 617 ATOM 494 CB TYR 124 24.590 61.220 20.349 1.00 41.20 1DLC 618 ATOM 495 CG TYR 124 23.913 61.533 21.674 1.00 45.22 1DLC 619 ATOM 496 CD1 TYR 124 24.551 62.322 22.634 1.00 46.84 1DLC 620 ATOM 497 CD2 TYR 124 22.643 61.038 21.972 1.00 46.22 1DLC 621 ATOM 498 CE1 TYR 124 23.948 62.606 23.856 1.00 48.97 1DLC 622 ATOM 499 CE2 TYR 124 22.025 61.320 23.199 1.00 48.29 1DLC 623 ATOM 500 CZ TYR 124 22.688 62.105 24.135 1.00 50.39 1DLC 624 ATOM 501 OH TYR 124 22.109 62.394 25.353 1.00 51.34 1DLC 625 ATOM 502 N ALA 125 25.775 59.545 22.738 1.00 38.41 1DLC 626 ATOM 503 CA ALA 125 26.442 59.468 24.033 1.00 36.03 1DLC 627 ATOM 504 C ALA 125 27.544 58.411 24.021 1.00 35.18 1DLC 628 ATOM 505 O ALA 125 28.569 58.567 24.676 1.00 36.66 1DLC 629 ATOM 506 CB ALA 125 25.429 59.169 25.127 1.00 36.03 1DLC 630 ATOM 507 N LYS 126 27.332 57.349 23.253 1.00 34.60 1DLC 631 ATOM 508 CA LYS 126 28.300 56.259 23.132 1.00 35.76 1DLC 632 ATOM 509 C LYS 126 29.519 56.726 22.325 1.00 36.46 1DLC 633 ATOM 510 O LYS 126 30.669 56.513 22.719 1.00 36.95 1DLC 634 ATOM 511 CB LYS 126 27.621 55.071 22.445 1.00 38.14 1DLC 635 ATOM 512 CG LYS 126 28.249 53.708 22.678 1.00 39.63 1DLC 636 ATOM 513 CD LYS 126 27.180 52.619 22.514 1.00 43.72 1DLC 637 ATOM 514 CE LYS 126 27.763 51.210 22.428 1.00 45.37 1DLC 638 ATOM 515 NZ LYS 126 28.477 50.752 23.655 1.00 48.58 1DLC 639 ATOM 516 N ASN 127 29.258 57.409 21.215 1.00 38.31 1DLC 640 ATOM 517 CA ASN 127 30.321 57.915 20.353 1.00 39.87 1DLC 641 ATOM 518 C ASN 127 31.184 58.966 21.032 1.00 38.46 1DLC 642 ATOM 519 O ASN 127 32.404 58.932 20.904 1.00 39.48 1DLC 643 ATOM 520 CB ASN 127 29.749 58.479 19.051 1.00 42.71 1DLC 644 ATOM 521 CG ASN 127 29.088 57.415 18.198 1.00 46.61 1DLC 645 ATOM 522 OD1 ASN 127 28.081 57.675 17.543 1.00 52.98 1DLC 646 ATOM 523 ND2 ASN 127 29.648 56.209 18.198 1.00 42.83 1DLC 647 ATOM 524 N LYS 128 30.563 59.911 21.733 1.00 38.09 1DLC 648 ATOM 525 CA LYS 128 31.349 60.929 22.415 1.00 39.08 1DLC 649 ATOM 526 C LYS 128 32.237 60.300 23.472 1.00 38.691DLC 650 ATOM 527 O LYS 128 33.415 60.642 23.577 1.00 42.45 1DLC 651 ATOM 528 CB LYS 128 30.495 62.006 23.071 1.00 41.87 1DLC 652 ATOM 529 CG LYS 128 31.380 62.951 23.880 1.00 46.08 1DLC 653 ATOM 530 CD LYS 128 30.689 64.221 24.295 1.00 49.62 1DLC 654 ATOM 531 CE LYS 128 31.726 65.260 24.666 1.00 47.91 1DLC 655 ATOM 532 NZ LYS 128 32.699 65.442 23.547 1.00 50.26 1DLC 656 ATOM 533 N ALA 129 31.668 59.381 24.248 1.00 34.82 1DLC 657 ATOM 534 CA ALA 129 32.420 58.691 25.287 1.00 33.08 1DLC 658 ATOM 535 C ALA 129 33.673 58.059 24.676 1.00 32.09 1DLC 659 ATOM 536 O ALA 129 34.793 58.278 25.150 1.00 31.18 1DLC 660 ATOM 537 CB ALA 129 31.552 57.628 25.953 1.00 30.56 1DLC 661 ATOM 538 N LEU 130 33.486 57.327 23.582 1.00 32.74 1DLC 662 ATOM 539 CA LEU 130 34.600 56.673 22.903 1.00 30.32 1DLC 663 ATOM 540 C LEU 130 35.640 57.669 22.407 1.00 31.27 1DLC 664 ATOM 541 O LEU 130 36.849 57.410 22.474 1.00 31.13 1DLC 665 ATOM 542 CB LEU 130 34.081 55.813 21.755 1.00 29.76 1DLC 666 ATOM 543 CG LEU 130 33.435 54.489 22.182 1.00 30.23 1DLC 667 ATOM 544 CD1 LEU 130 32.732 53.832 21.000 1.00 30.62 1DLC 668 ATOM 545 CD2 LEU 130 34.499 53.559 22.764 1.00 26.30 1DLC 669 ATOM 546 N ALA 131 35.166 58.829 21.960 1.00 32.32 1DLC 670 ATOM 547 CA ALA 131 36.046 59.883 21.460 1.00 32.99 1DLC 671 ATOM 548 C ALA 131 36.929 60.416 22.584 1.00 34.16 1DLC 672 ATOM 549 O ALA 131 38.145 60.515 22.427 1.00 37.33 1DLC 673 ATOM 550 CB ALA 131 35.229 61.008 20.847 1.00 31.10 1DLC 674 ATOM 551 N GLU 132 36.318 60.735 23.725 1.00 34.14 1DLC 675 ATOM 552 CA GLU 132 37.054 61.234 24.891 1.00 31.85 1DLC 676 ATOM 553 C GLU 132 38.128 60.232 25.296 1.00 30.73 1DLC 677 ATOM 554 O GLU 132 39.279 60.598 25.536 1.00 30.23 1DLC 678 ATOM 555 CB GLU 132 36.109 61.439 26.072 1.00 28.74 1DLC 679 ATOM 556 CG GLU 132 35.049 62.483 25.842 1.00 33.99 1DLC 680 ATOM 557 CD GLU 132 35.617 63.884 25.722 1.00 40.12 1DLC 681 ATOM 558 OE1 GLU 132 36.787 64.104 26.104 1.00 41.36 1DLC 682 ATOM 559 OE2 GLU 132 34.882 64.778 25.251 1.00 46.52 1DLC 683 ATOM 560 N LEU 133 37.739 58.961 25.320 1.00 31.50 1DLC 684 ATOM 561 CA LEU 133 38.627 57.866 25.692 1.00 32.60 1DLC 685 ATOM 562 C LEU 133 39.845 57.712 24.785 1.00 34.20 1DLC 686 ATOM 563 O LEU 133 40.930 57.388 25.261 1.00 34.43 1DLC 687 ATOM 564 CB LEU 133 37.833 56.561 25.795 1.00 30.47 1DLC 688 ATOM 565 CG LEU 133 36.896 56.525 27.009 1.00 30.33 1DLC 689 ATOM 566 CD1 LEU 133 35.766 55.538 26.796 1.00 26.58 1DLC 690 ATOM 567 CD2 LEU 133 37.693 56.206 28.271 1.00 24.25 1DLC 691 ATOM 568 N GLN 134 39.679 57.952 23.486 1.00 37.63 1DLC 692 ATOM 569 CA GLN 134 40.812 57.866 22.564 1.00 39.17 1DLC 693 ATOM 570 C GLN 134 41.814 58.949 22.945 1.00 36.45 1DLC 694 ATOM 571 O GLN 134 43.015 58.701 23.038 1.00 38.66 1DLC 695 ATOM 572 CB GLN 134 40.363 58.083 21.119 1.00 47.75 1DLC 696 ATOM 573 CG GLN 134 39.344 57.074 20.614 1.00 61.82 1DLC 697 ATOM 574 CD GLN 134 39.792 55.634 20.821 1.00 70.74 1DLC 698 ATOM 575 OE1 GLN 134 40.513 55.060 19.996 1.00 73.31 1DLC 699 ATOM 576 NE2 GLN 134 39.359 55.041 21.928 1.00 73.58 1DLC 700 ATOM 577 N GLY 135 41.301 60.147 23.207 1.00 32.99 1DLC 701 ATOM 578 CA GLY 135 42.156 61.255 23.599 1.00 32.54 1DLC 702 ATOM 579 C GLY 135 42.871 61.024 24.921 1.00 32.17 1DLC 703 ATOM 580 O GLY 135 44.039 61.378 25.080 1.00 34.18 1DLC 704 ATOM 581 N LEU 136 42.160 60.445 25.881 1.00 30.44 1DLC 705 ATOM 582 CA LEU 136 42.729 60.151 27.190 1.00 30.39 1DLC 706 ATOM 583 C LEU 136 43.818 59.084 27.081 1.00 31.99 1DLC 707 ATOM 584 O LEU 136 44.794 59.096 27.828 1.00 32.33 1DLC 708 ATOM 585 CB LEU 136 41.637 59.668 28.141 1.00 28.24 1DLC 709 ATOM 586 CG LEU 136 40.578 60.685 28.552 1.00 25.44 1DLC 710 ATOM 587 CD1 LEU 136 39.432 59.977 29.232 1.00 20.57 1DLC 711 ATOM 588 CD2 LEU 136 41.202 61.714 29.468 1.00 23.94 1DLC 712 ATOM 589 N GLN 137 43.644 58.159 26.144 1.00 34.65 1DLC 713 ATOM 590 CA GLN 137 44.612 57.091 25.937 1.00 36.83 1DLC 714 ATOM 591 C GLN 137 45.968 57.692 25.570 1.00 37.51 1DLC 715 ATOM 592 O GLN 137 46.980 57.410 26.221 1.00 35.29 1DLC 716 ATOM 593 CB GLN 137 44.138 56.152 24.829 1.00 39.14 1DLC 717 ATOM 594 CG GLN 137 44.992 54.905 24.664 1.00 43.17 1DLC 718 ATOM 595 CD GLN 137 44.607 54.094 23.445 1.00 45.19 1DLC 719 ATOM 596 OE1 GLN 137 43.460 54.127 22.989 1.00 47.54 1DLC 720 ATOM 597 NE2 GLN 137 45.562 53.355 22.911 1.00 46.02 1DLC 721 ATOM 598 N ASN 138 45.970 58.561 24.561 1.00 37.22 1DLC 722 ATOM 599 CA ASN 138 47.195 59.219 24.119 1.00 39.24 1DLC 723 ATOM 600 C ASN 138 47.872 59.935 25.281 1.00 36.46 1DLC 724 ATOM 601 O ASN 138 49.078 59.799 25.478 1.00 36.61 1DLC 725 ATOM 602 CB ASN 138 46.898 60.203 22.989 1.00 43.17 1DLC 726 ATOM 603 CG ASN 138 46.319 59.516 21.764 1.00 50.90 1DLC 727 ATOM 604 OD1 ASN 138 46.471 58.303 21.580 1.00 54.32 1DLC 728 ATOM 605 ND2 ASN 138 45.640 60.283 20.923 1.00 51.88 1DLC 729 ATOM 606 N ASN 139 47.079 60.639 26.085 1.00 33.80 1DLC 730 ATOM 607 CA ASN 139 47.601 61.358 27.247 1.00 31.83 1DLC 731 ATOM 608 C ASN 139 48.263 60.412 28.233 1.00 30.17 1DLC 732 ATOM 609 O ASN 139 49.350 60.691 28.733 1.00 29.01 1DLC 733 ATOM 610 CB ASN 139 46.485 62.115 27.969 1.00 32.59 1DLC 734 ATOM 611 CG ASN 139 45.928 63.270 27.154 1.00 37.15 1DLC 735 ATOM 612 OD1 ASN 139 45.081 64.014 27.634 1.00 42.84 1DLC 736 ATOM 613 ND2 ASN 139 46.392 63.425 25.926 1.00 35.37 1DLC 737 ATOM 614 N VAL 140 47.611 59.281 28.493 1.00 30.85 1DLC 738 ATOM 615 CA VAL 140 48.141 58.301 29.436 1.00 35.20 1DLC 739 ATOM 616 C VAL 140 49.421 57.652 28.911 1.00 35.66 1DLC 740 ATOM 617 O VAL 140 50.406 57.516 29.645 1.00 36.30 1DLC 741 ATOM 618 CB VAL 140 47.097 57.202 29.794 1.00 33.23 1DLC 742 ATOM 619 CG1 VAL 140 47.596 56.370 30.970 1.00 30.81 1DLC 743 ATOM 620 CG2 VAL 140 45.772 57.829 30.158 1.00 34.27 1DLC 744 ATOM 621 N GLU 141 49.412 57.280 27.635 1.00 36.48 1DLC 745 ATOM 622 CA GLU 141 50.575 56.655 27.016 1.00 37.87 1DLC 746 ATOM 623 C GLU 141 51.777 57.606 26.989 1.00 36.94 1DLC 747 ATOM 624 O GLU 141 52.868 57.250 27.451 1.00 36.22 1DLC 748 ATOM 625 CB GLU 141 50.223 56.142 25.613 1.00 39.44 1DLC 749 ATOM 626 CG GLU 141 49.194 55.010 25.647 1.00 46.15 1DLC 750 ATOM 627 CD GLU 141 48.815 54.460 24.273 1.00 50.50 1DLC 751 ATOM 628 OE1 GLU 141 48.932 55.189 23.255 1.00 48.49 1DLC 752 ATOM 629 OE2 GLU 141 48.377 53.286 24.225 1.00 52.05 1DLC 753 ATOM 630 N ASP 142 51.562 58.831 26.514 1.00 34.71 1DLC 754 ATOM 631 CA ASP 142 52.633 59.819 26.462 1.00 33.53 1DLC 755 ATOM 632 C ASP 142 53.214 59.998 27.849 1.00 32.09 1DLC 756 ATOM 633 O ASP 142 54.434 60.066 28.019 1.00 33.76 1DLC 757 ATOM 634 CB ASP 142 52.124 61.168 25.943 1.00 34.47 1DLC 758 ATOM 635 CG ASP 142 51.806 61.150 24.452 1.00 37.60 1DLC 759 ATOM 636 OD1 ASP 142 52.150 60.158 23.765 1.00 37.44 1DLC 760 ATOM 637 OD2 ASP 142 51.204 62.135 23.967 1.00 37.76 1DLC 761 ATOM 638 N TYR 143 52.336 60.020 28.847 1.00 29.85 1DLC 762 ATOM 639 CA TYR 143 52.770 60.180 30.228 1.00 31.12 1DLC 763 ATOM 640 C TYR 143 53.619 59.010 30.741 1.00 31.96 1DLC 764 ATOM 641 O TYR 143 54.655 59.221 31.373 1.00 29.33 1DLC 765 ATOM 642 CB TYR 143 51.569 60.394 31.162 1.00 29.85 1DLC 766 ATOM 643 CG TYR 143 51.951 60.326 32.627 1.00 28.37 1DLC 767 ATOM 644 CD1 TYR 143 52.705 61.347 33.220 1.00 27.51 1DLC 768 ATOM 645 CD2 TYR 143 51.631 59.207 33.397 1.00 26.05 1DLC 769 ATOM 646 CE1 TYR 143 53.135 61.251 34.532 1.00 25.76 1DLC 770 ATOM 647 CE2 TYR 143 52.057 59.101 34.716 1.00 26.39 1DLC 771 ATOM 648 CZ TYR 143 52.809 60.124 35.274 1.00 27.82 1DLC 772 ATOM 649 OH TYR 143 53.252 60.012 36.569 1.00 30.91 1DLC 773 ATOM 650 N VAL 144 53.156 57.784 30.499 1.00 34.31 1DLC 774 ATOM 651 CA VAL 144 53.863 56.587 30.951 1.00 35.26 1DLC 775 ATOM 652 C VAL 144 55.239 56.440 30.316 1.00 36.56 1DLC 776 ATOM 653 O VAL 144 56.205 56.111 31.008 1.00 37.15 1DLC 777 ATOM 654 CB VAL 144 53.033 55.298 30.720 1.00 35.68 1DLC 778 ATOM 655 CG1 VAL 144 53.836 54.065 31.131 1.00 32.11 1DLC 779 ATOM 656 CG2 VAL 144 51.747 55.363 31.529 1.00 33.51 1DLC 780 ATOM 657 N SER 145 55.341 56.699 29.011 1.00 37.88 1DLC 781 ATOM 658 CA SER 145 56.642 56.601 28.332 1.00 38.87 1DLC 782 ATOM 659 C SER 145 57.635 57.535 29.031 1.00 34.99 1DLC 783 ATOM 660 O SER 145 58.720 57.117 29.437 1.00 38.01 1DLC 784 ATOM 661 CB SER 145 56.534 56.951 26.834 1.00 39.91 1DLC 785 ATOM 662 OG SER 145 56.444 58.350 26.596 1.00 46.34 1DLC 786 ATOM 663 N ALA 146 57.207 58.772 29.258 1.00 30.82 1DLC 787 ATOM 664 CA ALA 146 58.031 59.761 29.931 1.00 30.30 1DLC 788 ATOM 665 C ALA 146 58.359 59.340 31.364 1.00 31.85 1DLC 789 ATOM 666 O ALA 146 59.509 59.426 31.790 1.00 35.45 1DLC 790 ATOM 667 CB ALA 146 57.345 61.123 29.915 1.00 27.74 1DLC 791 ATOM 668 N LEU 147 57.362 58.863 32.103 1.00 32.59 1DLC 792 ATOM 669 CA LEU 147 57.595 58.432 33.477 1.00 32.81 1DLC 793 ATOM 670 C LEU 147 58.607 57.297 33.490 1.00 33.53 1DLC 794 ATOM 671 O LEU 147 59.496 57.252 34.337 1.00 35.25 1DLC 795 ATOM 672 CB LEU 147 56.300 57.968 34.150 1.00 32.39 1DLC 796 ATOM 673 CG LEU 147 56.502 57.425 35.574 1.00 30.47 1DLC 797 ATOM 674 CD1 LEU 147 57.043 58.522 36.480 1.00 29.60 1DLC 798 ATOM 675 CD2 LEU 147 55.204 56.866 36.129 1.00 32.87 1DLC 799 ATOM 676 N SER 148 58.489 56.399 32.523 1.00 34.54 1DLC 800 ATOM 677 CA SER 148 59.400 55.270 32.416 1.00 38.01 1DLC 801 ATOM 678 C SER 148 60.844 55.766 32.240 1.00 38.45 1DLC 802 ATOM 679 O SER 148 61.767 55.311 32.931 1.00 38.67 1DLC 803 ATOM 680 CB SER 148 58.993 54.388 31.237 1.00 41.71 1DLC 804 ATOM 681 OG SER 148 59.823 53.242 31.146 1.00 52.18 1DLC 805 ATOM 682 N SER 149 61.031 56.724 31.338 1.00 37.6D 1DLC 806 ATOM 683 CA SER 149 62.355 57.292 31.098 1.00 36.97 1DLC 807 ATOM 684 C SER 149 62.888 57.943 32.369 1.00 36.69 1DLC 808 ATOM 685 O SER 149 64.015 57.693 32.768 1.00 40.93 1DLC 809 ATOM 686 CB SER 149 62.317 58.329 29.968 1.00 40.27 1DLC 810 ATOM 687 OG SER 149 61.927 57.753 28.725 1.00 42.78 1DLC 811 ATOM 688 N TRP 150 62.057 58.739 33.030 1.00 36.23 1DLC 812 ATOM 689 CA TRP 150 62.458 59.417 34.260 1.00 35.43 1DLC 813 ATOM 69D C TRP 150 62.997 58.455 35.332 1.00 40.04 1DLC 814 ATOM 691 O TRP 150 64.055 58.695 35.912 1.00 41.77 1DLC 815 ATOM 692 CB TRP 150 61.286 60.237 34.813 1.00 29.63 1DLC 816 ATOM 693 CG TRP 150 61.601 60.987 36.069 1.00 25.67 1DLC 817 ATOM 694 CD1 TRP 150 61.510 60.519 37.348 1.00 25.82 1DLC 818 ATOM 695 CD2 TRP 150 62.068 62.339 36.170 1.00 26.03 1DLC 819 ATOM 696 NE1 TRP 150 61.895 61.491 38.236 1.00 23.31 1DLC 820 ATOM 697 CE2 TRP 150 62.241 62.619 37.541 1.00 22.80 1DLC 821 ATOM 698 CE3 TRP 150 62.354 63.342 35.235 1.00 25.92 1DLC 822 ATOM 699 CZ2 TRP 150 62.687 63.857 38.001 1.00 25.85 1DLC 823 ATOM 700 CZ3 TRP 150 62.797 64.578 35.696 1.00 26.29 1DLC 824 ATOM 701 CH2 TRP 150 62.958 64.822 37.065 1.00 25.55 1DLC 825 ATOM 702 N GLN 151 62.263 57.378 35.602 1.00 44.57 1DLC 826 ATOM 703 CA GLN 151 62.687 56.396 36.602 1.00 48.28 1DLC 827 ATOM 704 C GLN 151 64.013 55.747 36.227 1.00 50.95 1DLC 828 ATOM 705 O GLN 151 64.902 55.586 37.061 1.00 50.37 1DLC 829 ATOM 706 CB GLN 151 61.627 55.304 36.763 1.00 48.02 1DLC 830 ATOM 707 CG GLN 151 60.751 55.460 37.990 1.00 51.89 1DLC 831 ATOM 708 CD GLN 151 61.539 55.351 39.287 1.00 55.39 1DLC 832 ATOM 709 OE1 GLN 151 62.270 54.382 39.506 1.00 56.87 1DLC 833 ATOM 710 NE2 GLN 151 61.397 56.345 40.153 1.00 54.44 1DLC 834 ATOM 711 N LYS 152 64.116 55.379 34.954 1.00 55.10 1DLC 835 ATOM 712 CA LYS 152 65.296 54.729 34.388 1.00 59.98 1DLC 836 ATOM 713 C LYS 152 66.545 55.624 34.404 1.00 62.63 1DLC 837 ATOM 714 O LYS 152 67.645 55.172 34.734 1.00 63.39 1DLC 838 ATOM 715 CB LYS 152 64.974 54.300 32.953 1.00 59.73 1DLC 839 ATOM 716 CG LYS 152 65.960 53.357 32.301 1.00 62.85 1DLC 840 ATOM 717 CD LYS 152 65.440 52.978 30.920 1.00 68.02 1DLC 841 ATOM 718 CE LYS 152 66.367 52.023 30.168 1.00 69.39 1DLC 842 ATOM 719 NZ LYS 152 65.842 51.764 28.785 1.00 68.57 1DLC 843 ATOM 720 N ASN 153 66.367 56.891 34.044 1.00 64.53 1DLC 844 ATOM 721 CA ASN 153 67.472 57.839 34.003 1.00 66.57 1DLC 845 ATOM 722 C ASN 153 67.961 58.271 35.384 1.00 68.87 1DLC 846 ATOM 723 O ASN 153 67.165 58.560 36.283 1.00 68.08 1DLC 847 ATOM 724 CB ASN 153 67.097 59.057 33.153 1.00 67.50 1DLC 848 ATOM 725 CG ASN 153 67.050 58.743 31.656 1.00 69.77 1DLC 849 ATOM 726 DD1 ASN 153 66.936 59.649 30.831 1.00 71.11 1DLC 850 ATOM 727 ND2 ASN 153 67.150 57.464 31.300 1.00 68.53 1DLC 8S1 ATOM 728 N PRO 154 69.294 58.308 35.570 1.00 71.40 1DLC 852 ATOM 729 CA PRO 154 69.934 58.697 36.830 1.00 71.82 1DLC 853 ATOM 730 C PRO 154 69.610 60.141 37.198 1.00 72.79 1DLC 854 ATOM 731 O PRO 154 69.311 60.961 36.324 1.00 73.90 1DLC 855 ATOM 732 CB PRO 154 71.424 58.545 36.516 1.00 71.42 1DLC 856 ATOM 733 CG PRO 154 71.450 57.498 35.443 1.00 71.51 1DLC 857 ATOM 734 CD PRO 154 70.312 57.939 34.570 1.00 71.69 1DLC 858 ATOM 735 N VAL 155 69.768 60.470 38.477 1.00 73.01 1DLC 859 ATOM 736 CA VAL 155 69.491 61.818 38.977 1.00 73.15 1DLC 860 ATOM 737 C VAL 155 70.486 62.875 38.445 1.00 75.28 1DLC 861 ATOM 738 O VAL 155 70.723 63.903 39.077 1.00 75.71 1DLC 862 ATOM 739 CB VAL 155 69.476 61.835 40.528 1.00 71.19 1DLC 863 ATOM 740 CG1 VAL 155 68.762 63.078 41.040 1.00 70.94 1DLC 864 ATOM 741 CG2 VAL 155 68.801 60.577 41.069 1.00 69.36 1DLC 865 ATOM 742 N SER 156 71.065 62.602 37.280 1.00 77.11 1DLC 866 ATOM 743 CA SER 156 72.021 63.495 36.635 1.00 78.87 1DLC 867 ATOM 744 C SER 156 71.400 64.161 35.408 1.00 79.29 1DLC 868 ATOM 745 O SER 156 71.396 65.386 35.299 1.00 82.25 1DLC 869 ATOM 746 CB SER 156 73.261 62.709 36.206 1.00 80.07 1DLC 870 ATOM 747 OG SER 156 72.912 61.680 35.287 1.00 82.65 1DLC 871 ATOM 748 N SER 157 70.853 63.352 34.500 1.00 76.97 1DLC 872 ATOM 749 CA SER 157 70.225 63.867 33.274 1.00 75.30 1DLC 873 ATOM 750 C SER 157 68.956 64.689 33.534 1.00 72.28 1DLC 874 ATOM 751 O SER 157 68.296 65.162 32.599 1.00 72.55 1DLC 875 ATOM 752 CB SER 157 69.896 62.715 32.317 1.00 78.07 1DLC 876 ATOM 753 OG SER 157 69.458 63.189 31.047 1.00 80.58 1DLC 877 ATOM 754 N ARG 158 68.597 64.824 34.805 1.00 67.95 1DLC 878 ATOM 755 CA ARG 158 67.422 65.585 35.193 1.00 62.74 1DLC 879 ATOM 756 C ARG 158 67.736 67.076 35.191 1.00 59.17 1DLC 880 ATOM 757 O ARG 158 68.229 67.636 36.170 1.00 60.26 1DLC 881 ATOM 758 CB ARG 158 66.933 65.122 36.561 1.00 62.84 1DLC 882 ATOM 759 CG ARG 158 66.524 63.677 36.539 1.00 64.01 1DLC 883 ATOM 760 CD ARG 158 66.356 63.122 37.919 1.00 64.75 1DLC 884 ATOM 761 NE ARG 158 66.051 61.699 37.848 1.00 67.56 1DLC 885 ATOM 762 CZ ARG 158 65.638 60.970 38.879 1.00 71.03 1DLC 886 ATOM 763 NH1 ARG 158 65.479 61.529 40.079 1.00 70.73 1DLC 887 ATOM 764 NH2 ARG 158 65.372 59.678 38.706 1.00 73.39 1DLC 888 ATOM 765 N ASN 159 67.500 67.692 34.045 1.00 52.90 1DLC 889 ATOM 766 CA ASN 159 67.737 69.110 33.868 1.00 46.95 1DLC 890 ATOM 767 C ASN 159 66.389 69.826 33.888 1.00 44.55 1DLC 891 ATOM 768 O ASN 159 65.351 69.202 33.666 1.00 45.26 1DLC 892 ATOM 769 CB ASN 159 68.435 69.331 32.532 1.00 45.92 1DLC 893 ATOM 770 CG ASN 159 67.630 68.811 31.374 1.00 40.97 1DLC 894 ATOM 771 OD1 ASN 159 66.694 69.453 30.928 1.00 44.27 1DLC 895 ATOM 772 ND2 ASN 159 67.971 67.632 30.898 1.00 42.45 1DLC 896 ATOM 773 N PRO 160 66.383 71.148 34.126 1.00 43.08 1DLC 897 ATOM 774 CA PRO 160 65.129 71.908 34.161 1.00 40.97 1DLC 898 ATOM 775 C PRO 160 64.253 71.635 32.942 1.00 40.72 1DLC 899 ATOM 776 O PRO 160 63.033 71.541 33.039 1.00 43.29 1DLC 900 ATOM 777 CB PRO 160 65.617 73.359 34.167 1.00 37.69 1DLC 901 ATOM 778 CG PRO 160 66.883 73.275 34.935 1.00 38.08 1DLC 902 ATOM 779 CD PRO 160 67.537 72.036 34.363 1.00 41.86 1DLC 903 ATOM 780 N HIS 161 64.898 71.454 31.800 1.00 41.25 1DLC 904 ATOM 781 CA HIS 161 64.199 71.210 30.551 1.00 41.19 1DLC 905 ATOM 782 C HIS 161 63.404 69.905 30.481 1.00 38.76 1DLC 906 ATOM 783 O HIS 161 62.324 69.880 29.901 1.00 40.73 1DLC 907 ATOM 784 CB HIS 161 65.191 71.365 29.393 1.00 46.06 1DLC 908 ATOM 785 CG HIS 161 64.907 70.490 28.220 1.00 51.42 1DLC 909 ATOM 786 ND1 HIS 161 63.840 70.697 27.371 1.00 53.89 1DLC 910 ATOM 787 CD2 HIS 161 65.564 69.405 27.749 1.00 54.97 1DLC 911 ATOM 788 CE1 HIS 161 63.851 69.775 26.428 1.00 57.18 1DLC 912 ATOM 789 NE2 HIS 161 64.887 68.979 26.633 1.00 60.77 1DLC 913 ATOM 790 N SER 162 63.927 68.824 31.048 1.00 37.14 1DLC 914 ATOM 791 CA SER 162 63.201 67.547 31.031 1.00 37.50 1DLC 915 ATOM 792 C SER 162 62.112 67.523 32.108 1.00 35.54 1DLC 916 ATOM 793 O SER 162 61.074 66.881 31.944 1.00 35.11 1DLC 917 ATOM 794 CB SER 162 64.147 66.347 31.188 1.00 35.89 1DLC 918 ATOM 795 CG SER 162 64.975 66.468 32.332 1.00 43.72 1DLC 919 ATOM 796 N GLN 163 62.349 68.245 33.197 1.00 33.11 1DLC 920 ATOM 797 CA GLN 163 61.382 68.351 34.283 1.00 34.19 1DLC 921 ATOM 798 C GLN 163 60.081 68.977 33.769 1.00 34.41 1DLC 922 ATOM 799 O GLN 163 58.986 68.508 34.072 1.00 35.10 1DLC 923 ATOM 800 CB GLN 163 61.924 69.248 35.385 1.00 31.93 1DLC 924 ATOM 801 CG GLN 163 63.188 68.789 36.034 1.00 31.11 1DLC 925 ATOM 802 CD GLN 163 63.564 69.707 37.178 1.00 37.44 1DLC 926 ATOM 803 OE1 GLN 163 63.862 69.258 38.281 1.00 39.60 1DLC 927 ATOM 804 NE2 GLN 163 63.508 71.009 36.932 1.00 39.57 1DLC 928 ATOM 805 N GLY 164 60.216 70.052 33.001 1.00 33.81 1DLC 929 ATOM 806 CA GLY 164 59.058 70.733 32.446 1.00 35.60 1DLC 930 ATOM 807 C GLY 164 58.297 69.918 31.416 1.00 35.04 1DLC 931 ATOM 808 O GLY 164 57.116 70.156 31.188 1.00 36.07 1DLC 932 ATOM 809 N ARG 165 58.985 68.971 30.785 1.00 36.94 1DLC 933 ATOM 810 CA ARG 165 58.392 68.094 29.774 1.00 38.83 1DLC 934 ATOM 811 C ARG 165 57.436 67.133 30.467 1.00 38.42 1DLC 935 ATOM 812 O ARG 165 56.289 66.960 30.043 1.00 41.35 1DLC 936 ATOM 813 CB ARG 165 59.496 67.291 29.061 1.00 43.60 1DLC 937 ATOM 814 CG ARG 165 59.010 66.120 28.187 1.00 49.27 1DLC 938 ATOM 815 CD ARG 165 60.160 65.155 27.855 1.00 55.07 1DLC 939 ATOM 816 NE ARG 165 59.759 64.046 26.979 1.00 59.97 1DLC 940 ATOM 817 CZ ARG 165 60.243 62.804 27.059 1.00 64.96 1DLC 941 ATOM 818 NH1 ARG 165 61.153 62.491 27.981 1.00 64.66 1DLC 942 ATOM 819 NH2 ARG 165 59.843 61.869 26.199 1.00 64.23 1DLC 943 ATOM 820 N ILE 166 57.915 66.523 31.548 1.00 35.09 1DLC 944 ATOM 821 CA ILE 166 57.118 65.572 32.310 1.00 33.64 1DLC 945 ATOM 822 C ILE 166 55.992 66.289 33.081 1.00 33.53 1DLC 946 ATOM 823 O ILE 166 54.861 65.806 33.128 1.00 31.99 1DLC 947 ATOM 824 CB ILE 166 58.024 64.698 33.236 1.00 30.93 1DLC 948 ATOM 825 CG1 ILE 166 57.315 63.392 33.595 1.00 30.98 1DLC 949 ATOM 826 CG2 ILE 166 58.432 65.459 34.481 1.00 24.94 1DLC 950 ATOM 827 CD1 ILE 166 58.200 62.399 34.321 1.00 34.42 1DLC 951 ATOM 828 N ARG 167 56.292 67.473 33.611 1.00 34.45 1DLC 952 ATOM 829 CA ARG 167 55.308 68.267 34.342 1.00 32.89 1DLC 953 ATOM 830 C ARG 167 54.109 68.617 33.476 1.00 34.17 1DLC 954 ATOM 831 O ARG 167 52.969 68.487 33.917 1.00 35.50 1DLC 955 ATOM 832 CB ARG 167 55.918 69.559 34.891 1.00 31.58 1DLC 956 ATOM 833 CG ARG 167 56.805 69.377 36.112 1.00 32.53 1DLC 957 ATOM 834 CD ARG 167 56.993 70.697 36.848 1.00 33.11 1DLC 958 ATOM 835 NE ARG 167 57.385 71.778 35.944 1.00 37.56 1DLC 959 ATOM 836 CZ ARG 167 58.639 72.165 35.720 1.00 35.70 1DLC 960 ATOM 837 NH1 ARG 167 59.647 71.567 36.335 1.00 35.92 1DLC 961 ATOM 838 NH2 ARG 167 58.883 73.154 34.873 1.00 36.61 1DLC 962 ATOM 839 N GLU 168 54.346 69.050 32.242 1.00 34.64 1DLC 963 ATOM 840 CA GLU 168 53.213 69.388 31.390 1.00 38.41 1DLC 964 ATOM 841 C GLU 168 52.484 68.185 30.790 1.00 37.42 1DLC 965 ATOM 842 O GLU 168 51.286 68.266 30.497 1.00 37.11 1DLC 966 ATOM 843 CB GLU 168 53.550 70.461 30.348 1.00 41.15 1DLC 967 ATOM 844 CG GLU 168 54.653 70.159 29.376 1.00 47.25 1DLC 968 ATOM 845 CD GLU 168 55.073 71.413 28.623 1.00 50.54 1DLC 969 ATOM 846 OE1 GLU 168 55.649 72.322 29.266 1.00 51.72 1DLC 970 ATOM 847 OE2 GLU 168 54.808 71.504 27.402 1.00 49.76 1DLC 971 ATOM 848 N LEU 169 53.187 67.065 30.639 1.00 35.43 1DLC 972 ATOM 849 CA LEU 169 52.553 65.849 30.137 1.00 33.88 1DLC 973 ATOM 850 C LEU 169 51.561 65.385 31.216 1.00 35.40 1DLC 974 ATOM 851 O LEU 169 50.422 64.987 30.921 1.00 33.65 1DLC 975 ATOM 852 CB LEU 169 53.593 64.752 29.876 1.00 34.42 1DLC 976 ATOM 853 CG LEU 169 54.409 64.833 28.582 1.00 32.40 1DLC 977 ATOM 854 CD1 LEU 169 55.219 63.568 28.399 1.00 29.86 1DLC 978 ATOM 855 CD2 LEU 169 53.477 65.002 27.412 1.00 30.50 1DLC 979 ATOM 856 N PHE 170 52.003 65.476 32.470 1.00 34.05 1DLC 980 ATOM 857 CA PHE 170 51.193 65.107 33.625 1.00 31.26 1DLC 981 ATOM 858 C PHE 170 49.989 66.045 33.765 1.00 31.02 1DLC 982 ATOM 859 O PHE 170 48.861 65.584 33.885 1.00 32.68 1DLC 983 ATOM 860 CB PHE 170 52.038 65.150 34.901 1.00 28.00 1DLC 984 ATOM 861 CG PHE 170 51.288 64.746 36.135 1.00 27.48 1DLC 985 ATOM 862 CD1 PHE 170 51.194 63.407 36.499 1.00 26.84 1DLC 986 ATOM 863 CD2 PHE 170 50.657 65.698 36.923 1.00 24.94 1DLC 987 ATOM 864 CE1 PHE 170 50.479 63.021 37.630 1.00 24.21 1DLC 988 ATOM 865 CE2 PHE 170 49.941 65.320 38.052 1.00 26.51 1DLC 989 ATOM 866 CZ PHE 170 49.852 63.977 38.405 1.00 24.66 1DLC 990 ATOM 867 N SER 171 50.231 67.356 33.759 1.00 31.26 1DLC 991 ATOM 868 CA SER 171 49.147 68.335 33.867 1.00 30.81 1DLC 992 ATOM 869 C SER 171 48.107 68.152 32.770 1.00 32.20 1DLC 993 ATOM 870 O SER 171 46.915 68.359 32.996 1.00 32.31 1DLC 994 ATOM 871 CB SER 171 49.681 69.766 33.821 1.00 30.26 1DLC 995 ATOM 872 OG SER 171 50.166 70.179 35.089 1.00 36.66 1DLC 996 ATOM 873 N GLN 172 48.563 67.781 31.577 1.00 31.91 1DLC 997 ATOM 874 CA GLN 172 47.659 67.552 30.455 1.00 33.14 1DLC 998 ATOM 875 C GLN 172 46.733 66.365 30.710 1.00 29.58 1DLC 999 ATOM 876 O GLN 172 45.516 66.488 30.614 1.00 30.17 1DLC1000 ATOM 877 CB GLN 172 48.445 67.330 29.155 1.00 37.12 1DLC1001 ATOM 878 CG GLN 172 48.917 68.614 28.486 1.00 45.43 1DLC1002 ATOM 879 CD GLN 172 47.759 69.492 28.022 1.00 49.43 1DLC1003 ATOM 880 OE1 GLN 172 46.967 69.099 27.163 1.00 52.00 1DLC1004 ATOM 881 NE2 GLN 172 47.660 70.688 28.586 1.00 49.43 1DLC1005 ATOM 882 N ALA 173 47.313 65.223 31.057 1.00 24.78 1DLC1006 ATOM 883 CA ALA 173 46.533 64.027 31.321 1.00 22.98 1DLC1007 ATOM 884 C ALA 173 45.524 64.270 32.442 1.00 24.72 1DLC1008 ATOM 885 O ALA 173 44.319 64.077 32.254 1.00 28.98 1DLC1009 ATOM 886 CB ALA 173 47.448 62.864 31.662 1.00 17.04 1DLC1010 ATOM 887 N GLU 174 46.007 64.756 33.583 1.00 22.65 1DLC1011 ATOM 888 CA GLU 174 45.153 65.032 34.739 1.00 22.62 1DLC1012 ATOM 889 C GLU 174 43.983 65.962 34.379 1.00 23.92 1DLC1013 ATOM 890 O GLU 174 42.821 65.690 34.703 1.00 24.12 1DLC1014 ATOM 891 CB GLU 174 45.993 65.646 35.862 1.00 20.71 1DLC1015 ATOM 892 CG GLU 174 45.347 65.635 37.245 1.00 27.17 1DLC1016 ATOM 893 CD GLU 174 44.233 66.665 37.422 1.00 26.70 1DLC1017 ATOM 894 OE1 GLU 174 44.464 67.856 37.132 1.00 30.91 1DLC1018 ATOM 895 OE2 GLU 174 43.129 66.287 37.864 1.00 25.52 1DLC1019 ATOM 896 N SER 175 44.301 67.045 33.684 1.00 25.54 1DLC1020 ATOM 897 CA SER 175 43.308 68.022 33.262 1.00 25.56 1DLC1021 ATOM 898 C SER 175 42.301 67.409 32.283 1.00 27.17 1DLC1022 ATOM 899 O SER 175 41.097 67.641 32.389 1.00 27.41 1DLC1023 ATOM 900 CB SER 175 44.006 69.214 32.611 1.00 23.74 1DLC1024 ATOM 901 OG SER 175 43.135 70.322 32.527 1.00 33.11 1DLC1025 ATOM 902 N HIS 176 42.794 66.593 31.354 1.00 29.90 1DLC1026 ATOM 903 CA HIS 176 41.941 65.937 30.364 1.00 30.36 1DLC1027 ATOM 904 C HIS 176 40.948 65.023 31.080 1.00 28.97 1DLC1028 ATOM 905 O HIS 176 39.793 64.905 30.675 1.00 29.85 1DLC1029 ATOM 906 CB HIS 176 42.795 65.139 29.367 1.00 34.90 1DLC1030 ATOM 907 CG HIS 176 42.059 64.703 28.131 1.00 46.08 1DLC1031 ATOM 908 ND1 HIS 176 40.692 64.506 28.094 1.00 49.82 1DLC1032 ATOM 909 CD2 HIS 176 42.510 64.405 26.888 1.00 48.94 1DLC1033 ATOM 910 CE1 HIS 176 40.335 64.107 26.886 1.00 50.00 1DLC1034 ATOM 911 NE2 HIS 176 41.421 64.036 26.135 1.00 50.95 1DLC1035 ATOM 912 N PHE 177 41.386 64.401 32.165 1.00 26.81 1DLC1036 ATOM 913 CA PHE 177 40.501 63.525 32.916 1.00 27.11 1DLC1037 ATOM 914 C PHE 177 39.326 64.261 33.562 1.00 25.34 1DLC1038 ATOM 915 O PHE 177 38.188 63.814 33.482 1.00 26.87 1DLC1039 ATOM 916 CB PHE 177 41.285 62.731 33.961 1.00 27.16 1DLC1040 ATOM 917 CG PHE 177 41.851 61.443 33.439 1.00 27.15 1DLC1041 ATOM 918 CD1 PHE 177 41.033 60.321 33.292 1.00 26.85 1DLC1042 ATOM 919 CD2 PHE 177 43.188 61.352 33.074 1.00 24.38 1DLC1043 ATOM 920 CE1 PHE 177 41.544 59.127 32.787 1.00 26.71 1DLC1044 ATOM 921 CE2 PHE 177 43.706 60.172 32.571 1.00 26.25 1DLC1045 ATOM 922 CZ PHE 177 42.882 59.055 32.426 1.00 27.48 1DLC1046 ATOM 923 N ARG 178 39.595 65.400 34.183 1.00 24.09 1DLC1047 ATOM 924 CA ARG 178 38.534 66.168 34.821 1.00 21.85 1DLC1048 ATOM 925 C ARG 178 37.544 66.715 33.796 1.00 25.36 1DLC1049 ATOM 926 O ARG 178 36.344 66.828 34.949 1.00 28.72 1DLC1050 ATOM 927 CB ARG 178 39.128 67.309 35.637 1.00 18.36 1DLC1051 ATOM 928 CG ARG 178 39.744 66.866 36.940 1.00 19.50 1DLC1052 ATOM 929 CD ARG 178 40.263 68.050 37.730 1.00 18.54 1DLC1053 ATOM 930 NE ARG 178 41.446 68.641 37.119 1.00 19.88 1DLC1054 ATOM 931 CZ ARG 178 41.544 69.911 36.742 1.00 23.68 1DLC1055 ATOM 932 NH1 ARG 178 40.522 70.739 36.906 1.00 25.01 1DLC1056 ATOM 933 NH2 ARG 178 42.669 70.356 36.202 1.00 22.04 1DLC1057 ATOM 934 N ASN 179 38.056 67.009 32.614 1.00 26.63 1DLC1058 ATOM 935 CA ASN 179 37.241 67.544 31.548 1.00 30.38 1DLC1059 ATOM 936 C ASN 179 36.323 66.476 30.938 1.00 32.76 1DLC1060 ATOM 937 O ASN 179 35.156 66.742 30.636 1.00 33.01 1DLC1061 ATOM 938 CB ASN 179 38.163 68.128 30.487 1.00 38.68 1DLC1062 ATOM 939 CG ASN 179 37.478 69.159 29.638 1.00 50.42 1DLC1063 ATOM 940 OD1 ASN 179 37.101 68.889 28.496 1.00 58.00 1DLC1064 ATOM 941 ND2 ASN 179 37.295 70.353 30.191 1.00 56.89 1DLC1065 ATOM 942 N SER 180 36.849 65.257 30.815 1.00 31.80 1DLC1066 ATOM 943 CA SER 180 36.123 64.128 30.229 1.00 29.25 1DLC1067 ATOM 944 C SER 180 35.138 63.345 31.101 1.00 28.52 1DLC1068 ATOM 945 O SER 180 34.139 62.844 30.592 1.00 29.31 1DLC1069 ATOM 946 CB SER 180 37.108 63.140 29.606 1.00 26.37 1DLC1070 ATOM 947 OG SER 180 37.889 63.786 28.624 1.00 28.28 1DLC1071 ATOM 948 N MET 181 35.411 63.222 32.397 1.00 25.80 1DLC1072 ATOM 949 CA MET 181 34.535 62.467 33.295 1.00 24.36 1DLC1073 ATOM 950 C MET 181 33.013 62.660 33.109 1.00 25.40 1DLC1074 ATOM 951 O MET 181 32.260 61.678 33.070 1.00 25.51 1DLC1075 ATOM 952 CB MET 181 34.939 62.674 34.760 1.00 19.33 1DLC1076 ATOM 953 CG MET 181 36.253 61.994 35.152 1.00 20.86 1DLC1077 ATOM 954 SD MET 181 36.411 60.263 34.634 1.00 21.66 1DLC1078 ATOM 955 CE MET 181 35.276 59.487 35.735 1.00 16.01 1DLC1079 ATOM 956 N PRO 182 32.545 63.913 32.954 1.00 25.51 1DLC1080 ATOM 957 CA PRO 182 31.103 64.138 32.772 1.00 25.99 1DLC1081 ATOM 958 C PRO 182 30.491 63.331 31.615 1.00 25.29 1DLC1082 ATOM 959 O PRO 182 29.311 63.003 31.640 1.00 27.08 1DLC1083 ATOM 960 CB PRO 182 31.031 65.640 32.507 1.00 25.60 1DLC1084 ATOM 961 CG PRO 182 32.160 66.174 33.318 1.00 23.18 1DLC1085 ATOM 962 CD PRO 182 33.264 65.200 33.017 1.00 25.77 1DLC1086 ATOM 963 N SER 183 31.303 63.000 30.617 1.00 24.96 1DLC1087 ATOM 964 CA SER 183 30.842 62.226 29.465 1.00 26.52 1DLC1088 ATOM 965 C SER 183 30.491 60.792 29.817 1.00 26.32 1DLC1089 ATOM 966 O SER 183 29.785 60.122 29.068 1.00 29.73 1DLC1090 ATOM 967 CB SER 183 31.899 62.204 28.356 1.00 25.87 1DLC1091 ATOM 968 OG SER 183 31.952 63.438 27.666 1.00 34.94 1DLC1092 ATOM 969 N PHE 184 31.025 60.300 30.928 1.00 26.09 1DLC1093 ATOM 970 CA PHE 184 30.754 58.928 31.357 1.00 25.51 1DLC1094 ATOM 971 C PHE 184 29.683 58.923 32.447 1.00 24.26 1DLC1095 ATOM 972 O PHE 184 29.529 57.957 33.188 1.00 24.61 1DLC1096 ATOM 973 CB PHE 184 32.039 58.266 31.859 1.00 23.91 1DLC1097 ATOM 974 CG PHE 184 33.248 58.594 31.031 1.00 25.50 1DLC1098 ATOM 975 CD1 PHE 184 33.228 58.437 29.648 1.00 25.62 1DLC1099 ATOM 976 CD2 PHE 184 34.402 59.085 31.630 1.00 23.80 1DLC1100 ATOM 977 CE1 PHE 184 34.339 58.767 28.876 1.00 26.43 1DLC1101 ATOM 978 CE2 PHE 184 35.515 59.418 30.866 1.00 24.57 1DLC1102 ATOM 979 CZ PHE 184 35.485 59.260 29.488 1.00 23.14 1DLC1103 ATOM 980 N ALA 185 28.925 60.007 32.522 1.00 23.06 1DLC1104 ATOM 981 CA ALA 185 27.879 60.119 33.518 1.00 24.13 1DLC1105 ATOM 982 C ALA 185 26.708 60.976 33.041 1.00 23.68 1DLC1106 ATOM 983 O ALA 185 26.076 61.650 33.841 1.00 27.10 1DLC1107 ATOM 984 CB ALA 185 28.461 60.681 34.803 1.00 19.53 1DLC1108 ATOM 985 N ILE 186 26.396 60.930 31.749 1.00 26.51 1DLC1109 ATOM 986 CA ILE 186 25.287 61.737 31.219 1.00 30.55 1DLC1110 ATOM 987 C ILE 186 23.923 61.273 31.738 1.00 31.15 1DLC1111 ATOM 988 O ILE 186 23.660 60.073 31.881 1.00 30.54 1DLC1112 ATOM 989 CB ILE 186 25.310 61.876 29.645 1.00 32.49 1DLC1113 ATOM 990 CG1 ILE 186 23.994 61.413 29.014 1.00 35.37 1DLC1114 ATOM 991 CG2 ILE 186 26.506 61.164 29.036 1.00 32.13 1DLC1115 ATOM 992 CD1 ILE 186 22.958 62.522 28.851 1.00 41.70 1DLC1116 ATOM 993 N SER 187 23.061 62.243 32.025 1.00 34.59 1DLC1117 ATOM 994 CA SER 187 21.730 61.969 32.570 1.00 35.55 1DLC1118 ATOM 995 C SER 187 20.948 60.887 31.836 1.00 32.95 1DLC1119 ATOM 996 O SER 187 20.761 60.942 30.620 1.00 33.44 1DLC1120 ATOM 997 CB SER 187 20.905 63.252 32.665 1.00 35.13 1DLC1121 ATOM 998 OG SER 187 19.848 63.077 33.595 1.00 42.12 1DLC1122 ATOM 999 N GLY 188 20.493 59.899 32.593 1.00 30.43 1DLC1123 ATOM 1000 CA GLY 188 19.761 58.799 32.001 1.00 28.56 1DLC1124 ATOM 1001 C GLY 188 20.642 57.624 31.609 1.00 28.57 1DLC1125 ATOM 1002 O GLY 188 20.135 56.536 31.335 1.00 31.17 1DLC1126 ATOM 1003 N TYR 189 21.957 57.821 31.584 1.00 27.24 1DLC1127 ATOM 1004 CA TYR 189 22.870 56.734 31.222 1.00 27.78 1DLC1128 ATOM 1005 C TYR 189 23.913 56.391 32.282 1.00 25.94 1DLC1129 ATOM 1006 O TYR 189 24.832 55.615 32.031 1.00 27.94 1DLC1130 ATOM 1007 CB TYR 189 23.541 57.031 29.883 1.00 30.52 1DLC1131 ATOM 1008 CG TYR 189 22.541 57.088 28.765 1.00 35.63 1DLC1132 ATOM 1009 CD1 TYR 189 21.957 55.925 28.280 1.00 37.70 1DLC1133 ATOM 1010 CD2 TYR 189 22.125 58.307 28.237 1.00 38.49 1DLC1134 ATOM 1011 CE1 TYR 189 20.979 55.967 27.302 1.00 44.20 1DLC1135 ATOM 1012 CE2 TYR 189 21.146 58.366 27.255 1.00 43.26 1DLC1136 ATOM 1013 CZ TYR 189 20.573 57.190 26.791 1.00 47.00 1DLC1137 ATOM 1014 OH TYR 189 19.593 57.227 25.816 1.00 53.52 1DLC1138 ATOM 1015 N GLU 190 23.719 56.921 33.484 1.00 24.53 1DLC1139 ATOM 1016 CA GLU 190 24.624 56.700 34.609 1.00 23.53 1DLC1140 ATOM 1017 C GLU 190 24.978 55.243 34.900 1.00 24.17 1DLC1141 ATOM 1018 O GLU 190 26.153 54.912 35.031 1.00 27.99 1DLC1142 ATOM 1019 CB GLU 190 24.068 57.352 35.872 1.00 24.72 1DLC1143 ATOM 1020 CG GLU 190 23.907 58.865 35.776 1.00 26.76 1DLC1144 ATOM 1021 CD GLU 190 22.541 59.318 35.278 1.00 25.80 1DLC1145 ATOM 1022 OE1 GLU 190 21.778 58.510 34.718 1.00 26.88 1DLC1146 ATOM 1023 OE2 GLU 190 22.219 60.502 35.471 1.00 30.62 1DLC1147 ATOM 1024N VAL 191 23.973 54.375 34.996 1.00 23.30 1DLC1148 ATOM 1025 CA VAL 191 24.207 52.952 35.272 1.00 19.79 1DLC1149 ATOM 1026 C VAL 191 24.897 52.243 34.108 1.00 19.46 1DLC1150 ATOM 1027 O VAL 191 25.799 51.432 34.308 1.00 22.56 1DLC1151 ATOM 1028 CB VAL 191 22.889 52.203 35.615 1.00 18.04 1DLC1152 ATOM 1029 CG1 VAL 191 23.163 50.719 35.865 1.00 18.90 1DLC1153 ATOM 1030 CG2 VAL 191 22.232 52.824 36.845 1.00 20.32 1DLC1154 ATOM 1031 N LEU 192 24.491 52.566 32.890 1.00 18 69 1DLC1155 ATOM 1032 CA LEU 192 25.082 51.941 31.717 1.00 19.74 1DLC1156 ATOM 1033 C LEU 192 26.572 52.295 31.545 1.00 20.71 1DLC1157 ATOM 1034 G LEU 192 27.359 51.487 31.061 1.00 21.17 1DLC1158 ATOM 1035 CB LEU 192 24.271 52.294 30.464 1.00 18.07 1DLC1159 ATOM 1036 CG LEU 192 22.806 51.827 30.419 1.00 20.22 1DLC1160 ATOM 1037 CD1 LEU 192 22.152 52.272 29.115 1.00 18.09 1DLC1161 ATOM 1038 CD2 LEU 192 22.717 50.312 30.547 1.00 20.02 1DLC1162 ATOM 1039 N PHE 193 26.955 53.496 31.962 1.00 20.56 1DLC1163 ATOM 1040 CA PHE 193 28.348 53.942 31.871 1.00 20.78 1DLC1164 ATOM 1041 C PHE 193 29.168 53.568 33.104 1.00 21.28 1DLC1165 ATOM 1042 O PHE 193 30.340 53.907 33.174 1.00 23.88 1DLC1166 ATOM 1043 CB PHE 193 28.408 55.470 31.765 1.00 20.19 1DLC1167 ATOM 1044 CG PHE 193 28.185 56.011 30.386 1.00 23.31 1DLC1168 ATOM 1045 CD1 PHE 193 29.016 55.646 29.333 1.00 20.93 1DLC1169 ATOM 1046 CD2 PHE 193 27.178 56.943 30.151 1.00 23.78 1DLC1170 ATOM 1047 CE1 PHE 193 28.848 56.205 28.066 1.00 23.90 1DLC1171 ATOM 1048 CE2 PHE 193 27.005 57.506 28.886 1.00 25.20 1DLC1172 ATOM 1049 CZ PHE 193 27.842 57.137 27.845 1.00 20.39 1DLC1173 ATOM 1050 N LEU 194 28.566 52.872 34.065 1.00 22.74 1DLC1174 ATOM 1051 CA LEU 194 29.242 52.536 35.324 1.00 21.21 1DLC1175 ATOM 1052 C LEU 194 30.634 51.887 35.302 1.00 21.36 1DLC1176 ATOM 1053 O LEU 194 31.533 52.328 36.019 1.00 20.76 1DLC1177 ATOM 1054 CB LEU 194 28.297 51.768 36.263 1.00 17.75 1DLC1178 ATOM 1055 CG LEU 194 28.574 51.962 37.766 1.00 16.29 1DLC1179 ATOM 1056 CD1 LEU 194 28.602 53.452 38.103 1.00 11.60 1DLC1180 ATOM 1057 CD2 LEU 194 27.528 51.257 38.608 1.00 12.55 1DLC1181 ATOM 1058 N THR 195 30.825 50.841 34.507 1.00 22.96 1DLC1182 ATOM 1059 CA THR 195 32.140 50.197 34.451 1.00 22.99 1DLC1183 ATOM 1060 C THR 195 33.160 51.083 33.716 1.00 22.92 1DLC1184 ATOM 1061 O THR 195 34.343 51.108 34.061 1.00 24.03 1DLC1185 ATOM 1062 CB THR 195 32.067 48.777 33.832 1.00 22.11 1DLC1186 ATOM 1063 OG1 THR 195 31.554 48.855 32.498 1.00 27.92 1DLC1187 ATOM 1064 CG2 THR 195 31.150 47.896 34.663 1.00 19.33 1DLC1188 ATOM 1065 N THR 196 32.681 51.845 32.738 1.00 19.98 1DLC1189 ATOM 1066 CA THR 196 33.521 52.768 31.987 1.00 19.69 1DLC1190 ATOM 1067 C THR 196 33.958 53.893 32.925 1.00 20.38 1DLC1191 ATOM 1068 O THR 196 35.132 54.233 32.983 1.00 25.74 1DLC1192 ATOM 1069 CB THR 196 32.748 53.374 30.805 1.00 21.39 1DLC1193 ATOM 1070 OG1 THR 196 32.366 52.330 29.903 1.00 23.90 1DLC1194 ATOM 1071 CG2 THR 196 33.598 54.387 30.064 1.00 22.13 1DLC1195 ATOM 1072 N TYR 197 33.011 54.457 33.671 1.00 20.18 1DLC1196 ATOM 1073 CA TYR 197 33.292 55.529 34.630 1.00 19.63 1DLC1197 ATOM 1074 C TYR 197 34.236 55.009 35.717 1.00 21.21 1DLC1198 ATOM 1075 O TYR 197 35.208 55.668 36.072 1.00 23.03 1DLC1199 ATOM 1076 CB TYR 197 31.986 56.019 35.271 1.00 18.30 1DLC1200 ATOM 1077 CG TYR 197 32.119 57.108 36.326 1.00 14.96 1DLC1201 ATOM 1078 CD1 TYR 197 32.471 56.799 37.639 1.00 16.47 1DLC1202 ATOM 1079 CD2 TYR 197 31.840 58.443 36.020 1.00 16.19 1DLC1203 ATOM 1080 CE1 TYR 197 32.540 57.784 38.620 1.00 16.31 1DLC1204 ATOM 1081 CE2 TYR 197 31.903 59.442 36.995 1.00 14.65 1DLC1205 ATOM 1082 CZ TYR 197 32.252 59.103 38.296 1.0C 18.45 1DLC1206 ATOM 1083 OH TYR 197 32.292 60.067 39.287 1.00 22.05 1DLC1207 ATOM 1084 N ALA 198 33.961 53.815 36.229 1.00 21.80 1DLC1208 ATOM 1085 CA ALA 198 34.793 53.225 37.277 1.00 21.41 1DLC1209 ATOM 1086 C ALA 198 36.259 53.101 36.852 1.00 20.73 1DLC1210 ATOM 1087 O ALA 198 37.157 53.523 37.579 1.00 19.18 1DLC1211 ATOM 1088 CB GLN 199 34.239 51.867 37.687 1.00 21.88 1DLC1212 ATOM 1089 N GLN 199 36.478 52.560 35.654 1.00 19.43 1DLC1213 ATOM 1090 CA GLN 199 37.816 52.374 35.100 1.00 19.21 1DLC1214 ATOM 1091 C GLN 199 38.515 53.708 34.780 1.00 21.06 1DLC1215 ATOM 1092 O GLN 199 39.726 53.849 34.969 1.00 22.54 1DLC1216 ATOM 1093 CB GLN 199 37.747 51.488 33.855 1.00 19.94 1DLC1217 ATOM 1094 CG GLN 199 37.211 50.082 34.106 1.00 21.16 1DLC1218 ATOM 1095 CD GLN 199 38.146 49.221 34.949 1.00 26.14 1DLC1219 ATOM 1096 OE1 GLN 199 39.348 49.465 35.003 1.00 28.88 1DLC1220 ATOM 1097 NE2 GLN 199 37.594 48.201 35.605 1.00 26.51 1DLC1221 ATOM 1098 N ALA 200 37.755 54.690 34.309 1.00 18.59 1DLC1222 ATOM 1099 CA ALA 200 38.318 56.002 34.006 1.00 17.37 1DLC1223 ATOM 1100 C ALA 200 38.668 56.712 35.316 1.00 19.35 1DLC1224 ATOM 1101 O ALA 200 39.754 57.287 35.455 1.00 22.44 1DLC1225 ATOM 1102 CB ALA 200 37.331 56.827 33.203 1.00 12.83 1DLC1226 ATOM 1103 N ALA 201 37.762 56.625 36.291 1.00 21.10 1DLC1227 ATOM 1104 CA ALA 201 37.946 57.232 37.612 1.00 18.23 1DLC1228 ATOM 1105 C ALA 201 39.206 56.667 38.259 1.00 18.71 1DLC1229 ATOM 1106 O ALA 201 40.045 57.404 38.769 1.00 22.55 1DLC1230 ATOM 1107 CB ALA 201 36.737 56.948 38.497 1.00 14.73 1DLC1231 ATOM 1108 N ASN 202 39.342 55.349 38.211 1.00 18.93 1DLC1232 ATOM 1109 CA ASN 202 40.506 54.674 38.773 1.00 19.98 1DLC1233 ATOM 1110 C ASN 202 41.795 55.231 38.172 1.00 20.62 1DLC1234 ATOM 1111 O ASN 202 42.723 55.601 38.897 1.00 20.33 1DLC1235 ATOM 1112 CB ASN 202 40.418 53.172 38.501 1.00 19.83 1DLC1236 ATOM 1113 CG ASN 202 41.612 52.418 39.032 1.00 19.77 1DLC1237 ATOM 1114 DD1 ASN 202 42.334 51.761 38.278 1.00 23.18 1DLC1238 ATOM 1115 ND2 ASN 202 41.835 52.509 40.332 1.00 14.55 1DLC1239 ATOM 1116 N THR 203 41.842 55.287 36.844 1.00 21.70 1DLC1240 ATOM 1117 CA THR 203 43.007 55.805 36.138 1.00 22.47 1DLC1241 ATOM 1118 C THR 203 43.322 57.223 36.631 1.00 23.03 1DLC1242 ATOM 1119 O THR 203 44.428 57.496 37.091 1.00 24.63 1DLC1243 ATOM 1120 CB THR 203 42.789 55.827 34.593 1.00 24.20 1DLC1244 ATOM 1121 DG1 THR 203 42.470 54.507 34.123 1.00 17.39 1DLC1245 ATOM 1122 CG2 THR 203 44.058 56.319 33.877 1.00 22.82 1DLC1246 ATOM 1123N HIS 204 42.318 58.091 36.619 1.00 20.16 1DLC1247 ATOM 1124 CA HIS 204 42.485 59.468 37.064 1.00 18.30 1DLC1248 ATOM 1125C HIS 204 43.123 59.566 38.451 1.00 19.42 1DLC1249 ATOM 1126 OHIS 204 44.064 60.328 38.651 1.00 23.12 1DLC1250 ATOM 1127 CB HIS 204 41.131 60.190 37.066 1.00 15.98 1DLC1251 ATOM 1128 CGHIS 204 41.224 61.664 37.314 1.00 15.26 1DLC1252 ATOM 1129 ND1HIS 204 40.123 62.443 37.582 1.00 18.22 1DLC1253 ATOM 1130CD2 HIS 204 42.285 62.508 37.302 1.00 14.66 1DLC1254 ATOM 1131 CE1HIS 204 40.495 63.703 37.719 1.00 17.73 1DLC1255 ATOM 1132 NE2HIS 204 41.803 63.768 37.554 1.00 15.61 1DLC1256 ATOM 1133 N LEU 205 42.603 58.810 39.410 1.00 19.20 1DLC1257 ATOM 1134 CA LEU 205 43.131 58.845 40.772 1.00 19.71 1DLC1258 ATOM 1135 C LEU 205 44.519 58.227 40.904 1.00 21.25 1DLC1259 ATOM 1136 O LEU 205 45.356 58.725 41.666 1.00 21.63 1DLC1260 ATOM 1137 CB LEU 205 42.168 58.161 41.745 1.00 18.84 1DLC1261 ATOM 1138 CG LEU 205 40.886 58.921 42.052 1.00 18.00 1DLC1262 ATOM 1139 CD1 LEU 205 40.010 58.052 42.908 1.00 20.41 1DLC1263 ATOM 1140 CD2 LEU 205 41.197 60.226 42.759 1.00 18.32 1DLC1264 ATOM 1141 N PHE 206 44.761 57.137 40.177 1.00 20.18 1DLC1265 ATOM 1142 CA PHE 206 46.060 56.477 40.233 1.00 20.34 1DLC1266 ATOM 1143 C PHE 206 47.117 57.423 39.677 1.00 20.04 1DLC1267 ATOM 1144 O PHE 206 48.221 57.522 40.192 1.00 21.09 1DLC1268 ATOM 1145 CB PHE 206 46.051 55.175 39.438 1.00 18.45 1DLC1269 ATOM 1146 CG PHE 206 47.169 54.263 39.798 1.00 16.28 1DLC1270 ATOM 1147 CD1 PHE 206 47.221 53.683 41.063 1.00 14.90 1DLC1271 ATOM 1148 CD2 PHE 206 48.196 54.006 38.897 1.00 16.65 1DLC1272 ATOM 1149 CE1 PHE 206 48.279 52.863 41.423 1.00 15.74 1DLC1273 ATOM 1150 CE2 PHE 206 49.259 53.185 39.247 1.00 14.95 1DLC1274 ATOM 1151 CZ PHE 206 49.303 52.612 40.510 1.00 13.30 1DLC1275 ATOM 1152 N LEU 207 46.737 58.124 38.621 1.00 21.24 1DLC1276 ATOM 1153 CA LEU 207 47.575 59.112 37.955 1.00 22.23 1DLC1277 ATOM 1154 C LEU 207 47.927 60.224 38.966 1.00 23.44 1DLC1278 ATOM 1155 O LEU 207 49.098 60.547 39.190 1.00 22.70 1DLC1279 ATOM 1156 CB LEU 207 46.758 59.698 36.801 1.00 23.02 1DLC1280 ATOM 1157 CG LEU 207 47.360 60.368 35.571 1.00 31.73 1DLC1281 ATOM 1158 CD1 LEU 207 47.968 61.698 35.942 1.00 33.70 1DLC1282 ATOM 1159 CD2 LEU 207 48.369 59.439 34.915 1.00 34.96 1DLC1283 ATOM 1160 N LEU 208 46.894 60.762 39.610 1.00 22.59 1DLC1284 ATOM 1161 CA LEU 208 47.044 61.837 40.584 1.00 20.00 1DLC1285 ATOM 1162 C LEU 208 48.056 61.607 41.704 1.00 20.94 1DLC1286 ATOM 1163 O LEU 208 48.819 62.514 42.046 1.00 22.20 1DLC1287 ATOM 1164 CB LEU 208 45.686 62.194 41.188 1.00 16.43 1DLC1288 ATOM 1165 CG LEU 208 44.872 63.256 40.452 1.00 17.48 1DLC1289 ATOM 1166 CD1 LEU 208 43.449 63.277 40.998 1.00 19.96 1DLC1290 ATOM 1167 CD2 LEU 208 45.527 64.630 40.597 1.00 13.67 1DLC1291 ATOM 1168 N LYS 209 48.073 60.410 42.282 1.00 20.58 1DLC1292 ATOM 1169 CA LYS 209 48.998 60.137 43.378 1.00 20.54 1DLC1293 ATOM 1170 C LYS 209 50.479 60.260 42.979 1.00 23.16 1DLC1294 ATOM 1171 O LYS 209 51.335 60.554 43.821 1.00 23.16 1DLC1295 ATOM 1172 CB LYS 209 48.672 58.798 44.057 1.00 16.68 1DLC1296 ATOM 1173 CG LYS 209 48.825 57.563 43.202 1.00 18.68 1DLC1297 ATOM 1174 CD LYS 209 50.232 57.019 43.295 1.00 18.58 1DLC1298 ATOM 1175 CE LYS 209 50.369 55.683 42.589 1.00 21.11 1DLC1299 ATOM 1176 NZ LYS 209 50.185 55.764 41.111 1.00 21.88 1DLC1300 ATOM 1177 N ASP 210 50.763 60.130 41.684 1.00 21.08 1DLC1301 ATOM 1178 CA ASP 210 52.131 60.261 41.191 1.00 19.70 1DLC1302 ATOM 1179 C ASP 210 52.703 61.647 41.503 1.00 20.97 1DLC1303 ATOM 1180 O ASP 210 53.907 61.798 41.741 1.00 21.99 1DLC1304 ATOM 1181 CB ASP 210 52.193 59.982 39.689 1.00 19.34 1DLC1305 ATOM 1182 CG ASP 210 52.109 58.504 39.366 1.00 19.19 1DLC1306 ATOM 1183 OD1 ASP 210 51.971 57.689 40.298 1.00 19.56 1DLC1307 ATOM 1184 OD2 ASP 210 52.205 58.153 38.178 1.00 21.76 1DLC1308 ATOM 1185 N ALA 211 51.829 62.650 41.540 1.00 19.23 1DLC1309 ATOM 1186 CA ALA 211 52.241 64.015 41.858 1.00 19.70 1DLC1310 ATOM 1187 C ALA 211 52.795 64.116 43.287 1.00 19.61 1DLC1311 ATOM 1188 O ALA 211 53.601 64.990 43.583 1.00 22.55 1DLC1312 ATOM 1189 CB ALA 211 51.072 64.979 41.680 1.00 15.73 1DLC1313 ATOM 1190 N GLN 212 52.365 63.227 44.177 1.00 18.98 1DLC1314 ATOM 1191 CA GLN 212 52.856 63.265 45.557 1.00 19.82 1DLC1315 ATOM 1192 C GLN 212 54.149 62.482 45.687 1.00 19.72 1DLC1316 ATOM 1193 O GLN 212 54.903 62.674 46.632 1.00 22.58 1DLC1317 ATOM 1194 CB GLN 212 51.819 62.718 46.556 1.00 15.61 1DLC1318 ATOM 1195 CG GLN 212 50.456 63.394 46.496 1.00 12.71 1DLC1319 ATOM 1196 CD GLN 212 50.538 64.903 46.573 1.00 12.86 1DLC1320 ATOM 1197 OE1 GLN 212 51.103 65.454 47.503 1.00 14.37 1DLC1321 ATOM 1198 NE2 GLN 212 49.964 65.578 45.593 1.00 10.00 1DLC1322 ATOM 1199 N ILE 213 54.389 61.582 44.741 1.00 22.18 1DLC1323 ATOM 1200 CA ILE 213 55.594 60.767 44.752 1.00 20.68 1DLC1324 ATOM 1201 C ILE 213 56.754 61.481 44.057 1.00 22.54 1DLC1325 ATOM 1202 O ILE 213 57.836 61.622 44.623 1.00 23.78 1DLC1326 ATOM 1203 CB ILE 213 55.356 59.419 44.054 1.00 20.69 1DLC1327 ATOM 1204 CG1 ILE 213 54.347 58.579 44.840 1.00 17.63 1DLC1328 ATOM 1205 CG2 ILE 213 56.670 58.666 43.909 1.00 25.19 1DLC1329 ATOM 1206 CD1 ILE 213 54.045 57.240 44.188 1.00 12.68 1DLC1330 ATOM 1207 N TYR 214 56.508 61.952 42.838 1.00 23.00 1DLC1331 ATOM 1208 CA TYR 214 57.528 62.631 42.043 1.00 22.33 1DLC1332 ATOM 1209 C TYR 214 57.425 64.154 41.979 1.00 24.14 1DLC1333 ATOM 1210 O TYR 214 58.269 64.801 41.374 1.00 28.23 1DLC1334 ATOM 1211 CB TYR 214 57.488 62.100 40.615 1.00 23.32 1DLC1335 ATOM 1212 CG TYR 214 57.727 60.620 40.479 1.00 26.06 1DLC1336 ATOM 1213 CD1 TYR 214 59.009 60.092 40.618 1.00 27.10 1DLC1337 ATOM 1214 CD2 TYR 214 56.678 59.746 40.184 1.00 25.78 1DLC1338 ATOM 1215 CE1 TYR 214 59.249 58.728 40.466 1.00 32.00 1DLC1339 ATOM 1216 CE2 TYR 214 56.907 58.374 40.026 1.00 31.14 1DLC1340 ATOM 1217 CZ TYR 214 58.199 57.874 40.169 1.00 32.77 1DLC1341 ATOM 1218 OH TYR 214 58.452 56.529 40.017 1.00 37.11 1DLC1342 ATOM 1219 N GLY 215 56.398 64.724 42.596 1.00 25.34 1DLC1343 ATOM 1220 CA GLY 215 56.198 66.166 42.560 1.00 27.83 1DLC1344 ATOM 1221 C GLY 215 57.419 67.067 42.648 1.00 29.47 1DLC1345 ATOM 1222 O GLY 215 57.663 67.867 41.746 1.00 28.30 1DLC1346 ATOM 1223 N GLU 216 58.174 66.954 43.737 1.00 32.54 1DLC1347 ATOM 1224 CA GLU 216 59.368 67.769 43.918 1.00 36.48 1DLC1348 ATOM 1225 C GLU 216 60.485 67.450 42.917 1.00 35.87 1DLC1349 ATOM 1226 O GLU 216 61.148 68.358 42.427 1.00 36.74 1DLC1350 ATOM 1227 CB GLU 216 59.878 67.676 45.351 1.00 41.84 1DLC1351 ATOM 1228 CG GLU 216 58.947 68.318 46.371 1.00 54.52 1DLC1352 ATOM 1229 CD GLU 216 59.656 68.698 47.671 1.00 64.18 1DLC1353 ATOM 1230 OE1 GLU 216 60.560 67.944 48.116 1.00 67.77 1DLC1354 ATOM 1231 OE2 GLU 216 59.311 69.764 48.244 1.00 67.98 1DLC1355 ATOM 1232 N GLU 217 60.665 66.172 42.591 1.00 34.29 1DLC1356 ATOM 1233 CA GLU 217 61.682 65.750 41.623 1.00 33.09 1DLC1357 ATOM 1234 C GLU 217 61.440 66.442 40.282 1.00 33.15 1DLC1358 ATOM 1235 O GLU 217 62.376 66.884 39.619 1.00 34.29 1DLC1359 ATOM 1236 CB GLU 217 61.617 64.238 41.385 1.00 36.76 1DLC1360 ATOM 1237 CG GLU 217 61.993 63.362 42.565 1.00 36.91 1DLC1361 ATOM 1238 CD GLU 217 62.121 61.887 42.182 1.00 39.24 1DLC1362 ATOM 1239 OE1 GLU 217 61.938 61.540 40.993 1.00 37.21 1DLC1363 ATOM 1240 OE2 GLU 217 62.416 61.067 43.074 1.00 42.79 1DLC1364 ATOM 1241 N TRP 218 60.172 66.488 39.878 1.00 31.27 1DLC1365 ATOM 1242 CA TRP 218 59.756 67.116 38.627 1.00 25.69 1DLC1366 ATOM 1243 C TRP 218 59.846 68.638 38.714 1.00 22.53 1DLC1367 ATOM 1244 O TRP 218 59.670 69.330 37.722 1.00 23.72 1DLC1368 ATOM 1245 CB TRP 218 58.312 66.720 38.282 1.00 26.69 1DLC1369 ATOM 1246 CG TRP 218 58.097 65.248 37.980 1.00 26.77 1DLC1370 ATOM 1247 CD1 TRP 218 59.051 64.322 37.664 1.00 28.09 1DLC1371 ATOM 1248 CD2 TRP 218 56.840 64.549 37.961 1.00 25.69 1DLC1372 ATOM 1249 NE1 TRP 218 58.468 63.093 37.449 1.00 28.06 1DLC1373 ATOM 1250 CE2 TRP 218 57.114 63.203 37.626 1.00 26.57 1DLC1374 ATOM 1251 CE3 TRP 218 55.512 64.929 38.196 1.00 22.74 1DLC1375 ATOM 1252 CZ2 TRP 218 56.102 62.235 37.519 1.00 25.71 1DLC1376 ATOM 1253 CZ3 TRP 218 54.511 63.967 38.089 1.00 21.96 1DLC1377 ATOM 1254 CH2 TRP 218 54.813 62.637 37.755 1.00 22.35 1DLC1378 ATOM 1255 N GLY 219 60.088 69.160 39.910 1.00 21.50 1DLC1379 ATOM 1256 CA GLY 219 60.192 70.595 40.068 1.00 22.27 1DLC1380 ATOM 1257 C GLY 219 58.871 71.338 40.117 1.00 27.62 1DLC1381 ATOM 1258 O GLY 219 58.757 72.444 39.593 1.00 31.08 1DLC1382 ATOM 1259 N TYR 220 57.852 70.712 40.696 1.00 30.00 1DLC1383 ATOM 1260 CA TYR 220 56.543 71.343 40.843 1.00 26.76 1DLC1384 ATOM 1261 C TYR 220 56.611 72.221 42.088 1.00 28.73 1DLC1385 ATOM 1262 O TYR 220 57.304 71.886 43.054 1.00 27.48 1DLC1386 ATOM 1263 CB TYR 220 55.453 70.289 41.076 1.00 27.42 1DLC1387 ATOM 1264 CG TYR 220 54.625 69.913 39.873 1.00 23.12 1DLC1388 ATOM 1265 CD1 TYR 220 53.951 70.881 39.130 1.00 21.42 1DLC1389 ATOM 1266 CD2 TYR 220 54.487 68.576 39.496 1.00 23.42 1DLC1390 ATOM 1267 CE1 TYR 220 53.152 70.521 38.034 1.00 22.62 1DLC1391 ATOM 1268 CE2 TYR 220 53.698 68.207 38.413 1.00 20.38 1DLC1392 ATOM 1269 CZ TYR 220 53.033 69.178 37.685 1.00 22.10 1DLC1393 ATOM 1270 OH TYR 220 52.252 68.802 36.617 1.00 23.88 1DLC1394 ATOM 1271 N GLU 221 55.870 73.324 42.080 1.00 30.82 1DLC1395 ATOM 1272 CA GLU 221 55.825 74.225 43.233 1.00 32.66 1DLC1396 ATOM 1273 C GLU 221 55.123 73.517 44.398 1.00 30.03 1DLC1397 ATOM 1274 O GLU 221 54.287 72.638 44.182 1.00 27.72 1DLC1398 ATOM 1275 CB GLU 221 55.023 75.492 42.894 1.00 38.56 1DLC1399 ATOM 1276 CG GLU 221 55.470 76.271 41.656 1.00 43.49 1DLC1400 ATOM 1277 CD GLU 221 56.855 76.898 41.791 1.00 48.97 1DLC1401 ATOM 1278 OE1 GLU 221 57.330 77.133 42.935 1.00 48.86 1DLC1402 ATOM 1279 OE2 GLU 221 57.468 77.163 40.730 1.00 52.79 1DLC1403 ATOM 1280 N LYS 222 55.454 73.909 45.624 1.00 30.89 1DLC1404 ATOM 1281 CA LYS 222 54.823 73.341 46.823 1.00 33.36 1DLC1405 ATOM 1282 C LYS 222 53.298 73.481 46.711 1.00 33.05 1DLC1406 ATOM 1283 O LYS 222 52.553 72.577 47.082 1.00 33.57 1DLC1407 ATOM 1284 CB LYS 222 55.281 74.096 48.072 1.00 36.59 1DLC1408 ATOM 1285 CG LYS 222 56.696 73.829 48.528 1.00 41.95 1DLC1409 ATOM 1286 CD LYS 222 56.774 72.524 49.300 1.00 52.08 1DLC1410 ATOM 1287 CE LYS 222 57.623 72.678 50.563 1.00 56.91 1DLC1411 ATOM 1288 NZ LYS 222 57.030 73.645 51.546 1.00 59.58 1DLC1412 ATOM 1289 N GLU 223 52.865 74.631 46.188 1.00 31.86 1DLC1413 ATOM 1290 CA GLU 223 51.453 74.964 45.985 1.00 30.30 1DLC1414 ATOM 1291 C GLU 223 50.767 74.012 45.016 1.00 28.77 1DLC1415 ATOM 1292 O GLU 223 49.592 73.689 45.192 1.00 30.14 1DLC1416 ATOM 1293 CB GLU 223 51.303 76.382 45.430 1.00 32.15 1DLC1417 ATOM 1294 CG GLU 223 51.827 77.493 46.326 1.00 39.10 1DLC1418 ATOM 1295 CD GLU 223 53.302 77.826 46.105 1.00 39.68 1DLC1419 ATOM 1296 OE1 GLU 223 53.980 77.137 45.315 1.00 36.48 1DLC1420 ATOM 1297 OE2 GLU 223 53.777 78.807 46.719 1.00 44.29 1DLC1421 ATOM 1298 N ASP 224 51.488 73.622 43.964 1.00 26.06 1DLC1422 ATOM 1299 CA ASP 224 50.975 72.702 42.946 1.00 26.67 1DLC1423 ATOM 1300 C ASP 224 50.699 71.311 43.509 1.00 25.47 1DLC1424 ATOM 1301 O ASP 224 49.610 70.763 43.347 1.00 26.25 1DLC1425 ATOM 1302 CB ASP 224 51.964 72.578 41.787 1.00 29.40 1DLC1426 ATOM 1303 CG ASP 224 52.088 73.860 40.979 1.00 38.45 1DLC1427 ATOM 1304 OD1 ASP 224 51.145 74.677 40.990 1.00 38.89 1DLC1428 ATOM 1305 OD2 ASP 224 53.134 74.052 40.319 1.00 45.08 1DLC1429 ATOM 1306 N ILE 225 51.684 70.762 44.205 1.00 21.39 1DLC1430 ATOM 1307 CA ILE 225 51.565 69.439 44.792 1.00 21.79 1DLC1431 ATOM 1308 C ILE 225 50.400 69.397 45.784 1.00 20.00 1DLC1432 ATOM 1309 O ILE 225 49.636 68.438 45.813 1.00 19.14 1DLC1433 ATOM 1310 CB ILE 225 52.901 69.030 45.465 1.00 20.50 1DLC1434 ATOM 1311 CG1 ILE 225 54.034 69.121 44.438 1.00 21.29 1DLC1435 ATOM 1312 CG2 ILE 225 52.819 67.608 46.001 1.00 20.23 1DLC1436 ATOM 1313 CD1 ILE 225 55.407 69.056 45.037 1.00 21.75 1DLC1437 ATOM 1314 N ALA 226 50.239 70.479 46.538 1.00 19.79 1DLC1438 ATOM 1315 CA ALA 226 49.166 70.610 47.524 1.00 20.24 1DLC1439 ATOM 1316 C ALA 226 47.782 70.704 46.854 1.00 21.11 1DLC1440 ATOM 1317 O ALA 226 46.799 70.134 47.341 1.00 18.19 1DLC1441 ATOM 1318 CB ALA 226 49.414 71.836 48.403 1.00 16.06 1DLC1442 ATOM 1319 N GLU 227 47.711 71.436 45.744 1.00 19.52 1DLC1443 ATOM 1320 CA GLU 227 46.460 71.572 45.019 1.00 19.61 1DLC1444 ATOM 1321 C GLU 227 46.075 70.210 44.465 1.00 21.10 1DLC1445 ATOM 1322 O GLU 227 44.900 69.838 44.492 1.00 26.53 1DLC1446 ATOM 1323 CB GLU 227 46.584 72.584 43.885 1.00 19.91 1DLC1447 ATOM 1324 CG GLU 227 45.303 72.736 43.075 1.00 21.72 1DLC1448 ATOM 1325 CD GLU 227 45.386 73.811 42.014 1.00 26.65 1DLC1449 ATOM 1326 OE1 GLU 227 46.212 74.736 42.159 1.00 30.03 1DLC1450 ATOM 1327 OE2 GLU 227 44.613 73.734 41.033 1.00 27.79 1DLC1451 ATOM 1328 N PHE 228 47.068 69.460 43.987 1.00 20.19 1DLC1452 ATOM 1329 CA PHE 228 46.832 68.114 43.456 1.00 18.86 1DLC1453 ATOM 1330 C PHE 228 46.335 67.182 44.569 1.00 19.65 1DLC1454 ATOM 1331 O PHE 228 45.418 66.387 44.361 1.00 20.81 1DLC1455 ATOM 1332 CB PHE 228 48.102 67.523 42.832 1.00 15.98 1DLC1456 ATOM 1333 CG PHE 228 48.416 68.035 41.445 1.00 14.18 1DLC1457 ATOM 1334 CD1 PHE 228 47.425 68.103 40.466 1.00 9.27 1DLC1458 ATOM 1335 CD2 PHE 228 49.726 68.404 41.108 1.00 12.83 1DLC1459 ATOM 1336 CE1 PHE 228 47.729 68.523 39.178 1.00 8.69 1DLC1460 ATOM 1337 CE2 PHE 228 50.047 68.829 39.816 1.00 9.25 1DLC1461 ATOM 1338 CZ PHE 228 49.049 68.887 38.849 1.00 13.45 1DLC1462 ATOM 1339 N TYR 229 46.919 67.297 45.757 1.00 17.04 1DLC1463 ATOM 1340 CA TYR 229 46.503 66.451 46.867 1.00 17.31 1DLC1464 ATOM 1341 C TYR 229 45.048 66.729 47.261 1.00 20.11 1DLC1465 ATOM 1342 O TYR 229 44.249 65.798 47.369 1.00 23.73 1DLC1466 ATOM 1343 CB TYR 229 47.426 66.625 48.072 1.00 13.52 1DLC1467 ATOM 1344 CG TYR 229 47.095 65.691 49.217 1.00 10.64 1DLC1468 ATOM 1345 CD1 TYR 229 47.277 64.319 49.094 1.00 9.77 1DLC1469 ATOM 1346 CD2 TYR 229 46.575 66.178 50.412 1.00 10.19 1DLC1470 ATOM 1347 CE1 TYR 229 46.947 63.455 50.131 1.00 9.80 1DLC1471 ATOM 1348 CE2 TYR 229 46.242 65.320 51.453 1.00 12.10 1DLC1472 ATOM 1349 CZ TYR 229 46.431 63.961 51.304 1.00 11.99 1DLC1473 ATOM 1350 OH TYR 229 46.106 63.107 52.330 1.00 16.85 1DLC1474 ATOM 1351 N LYS 230 44.693 67.998 47.462 1.00 19.47 1DLC1475 ATOM 1352 CA LYS 230 43.313 68.326 47.818 1.00 19.61 1DLC1476 ATOM 1353 C LYS 230 42.357 67.868 46.723 1.00 19.13 1DLC1477 ATOM 1354 O LYS 230 41.259 67.382 47.008 1.00 20.93 1DLC1478 ATOM 1355 CB LYS 230 43.137 69.812 48.083 1.00 17.36 1DLC1479 ATOM 1356 CG LYS 230 43.786 70.262 49.367 1.00 22.08 1DLC1480 ATOM 1357 CD LYS 230 43.346 71.657 49.735 1.00 22.71 1DLC1481 ATOM 1358 CE LYS 230 41.854 71.690 49.992 1.00 22.53 1DLC1482 ATOM 1359 NZ LYS 230 41.408 73.051 50.364 1.00 25.70 1DLC1483 ATOM 1360 N ARG 231 42.794 67.975 45.474 1.00 15.74 1DLC1484 ATOM 1361 CA ARG 231 41.972 67.527 44.366 1.00 16.22 1DLC1485 ATOM 1362 C ARG 231 41.786 66.011 44.455 1.00 17.99 1DLC1486 ATOM 1363 O ARG 231 40.698 65.508 44.202 1.00 20.26 1DLC1487 ATOM 1364 CB ARG 231 42.615 67.904 43.033 1.00 20.80 1DLC1488 ATOM 1365 CG ARG 231 41.890 67.346 41.811 1.00 20.81 1DLC1489 ATOM 1366 CD ARG 231 42.356 68.028 40.534 1.00 25.62 1DLC1490 ATOM 1367 NE ARG 231 42.219 69.481 40.616 1.00 25.19 1DLC1491 ATOM 1368 CZ ARG 231 43.158 70.346 40.247 1.00 24.34 1DLC1492 ATOM 1369 NH1 ARG 231 44.314 69.913 39.760 1.00 25.84 1DLC1493 ATOM 1370 NH2 ARG 231 42.947 71.648 40.390 1.00 23.15 1DLC1494 ATOM 1371 N GLN 232 42.838 65.293 44.852 1.00 16.37 1DLC1495 ATOM 1372 CA GLN 232 42.779 63.840 44.982 1.00 14.65 1DLC1496 ATOM 1373 C GLN 232 41.786 63.422 46.068 1.00 16.33 1DLC1497 ATOM 1374 O GLN 232 41.011 62.491 45.883 1.00 19.48 1DLC1498 ATOM 1375 CB GLN 232 44.160 63.255 45.289 1.00 13.62 1DLC1499 ATOM 1376 CG GLN 232 44.250 61.761 45.006 1.00 16.45 1DLC1500 ATOM 1377 CD GLN 232 45.507 61.102 45.540 1.00 18.66 1DLC1501 ATOM 1378 OE1 GLN 232 45.465 59.968 46.006 1.00 21.82 1DLC1502 ATOM 1379 NE2 GLN 232 46.631 61.797 45.468 1.00 17.44 1DLC1503 ATOM 1380 N LEU 233 41.812 64.114 47.201 1.00 13.18 1DLC1504 ATOM 1381 CA LEU 233 40.888 63.820 48.289 1.00 15.87 1DLC1505 ATOM 1382 C LEU 233 39.427 64.066 47.879 1.00 17.22 1DLC1506 ATOM 1383 O LEU 233 38.549 63.248 48.157 1.00 22.21 1DLC1507 ATOM 1384 CB LEU 233 41.209 64.679 49.507 1.00 14.55 1DLC1508 ATOM 1385 CG LEU 233 42.582 64.520 50.148 1.00 18.77 1DLC1509 ATOM 1386 CD1 LEU 233 42.837 65.712 51.054 1.00 21.30 1DLC1510 ATOM 1387 CD2 LEU 233 42.664 63.219 50.918 1.00 17.59 1DLC1511 ATOM 1388 N LYS 234 39.166 65.191 47.222 1.00 16.53 1DLC1512 ATOM 1389 CA LYS 234 37.811 65.504 46.802 1.00 17.73 1DLC1513 ATOM 1390 C LYS 234 37.280 64.450 45.831 1.00 18.98 1DLC1514 ATOM 1391 O LYS 234 36.177 63.925 46.003 1.00 20.56 1DLC1515 ATOM 1392 CB LYS 234 37.748 66.882 46.145 1.00 19.54 1DLC1516 ATOM 1393 CG LYS 234 36.316 67.360 45.891 1.00 30.78 1DLC1517 ATOM 1394 CD LYS 234 36.236 68.364 44.747 1.00 39.43 1DLC1518 ATOM 1395 CE LYS 234 36.703 67.727 43.433 1.00 48.46 1DLC1519 ATOM 1396 NZ LYS 234 36.739 68.660 42.257 1.00 52.24 1DLC1520 ATOM 1397 N LEU 235 38.080 64.119 44.825 1.00 19.47 1DLC1521 ATOM 1398 CA LEU 235 37.677 63.142 43.826 1.00 16.47 1DLC1522 ATOM 1399 C LEU 235 37.536 61.714 44.346 1.00 16.10 1DLC1523 ATOM 1400 O LEU 235 36.694 60.961 43.862 1.00 19.12 1DLC1524 ATOM 1401 CB LEU 235 38.593 63.224 42.604 1.00 17.24 1DLC1525 ATOM 1402 CG LEU 235 38.518 64.594 41.903 1.00 18.14 1DLC1526 ATOM 1403 CD1 LEU 235 39.500 64.684 40.746 1.00 17.32 1DLC1527 ATOM 1404 CD2 LEU 235 37.100 64.843 41.415 1.00 19.19 1DLC1528 ATOM 1405 N THR 236 38.324 61.337 45.347 1.00 15.47 1DLC1529 ATOM 1406 CA THR 236 38.200 59.988 45.915 1.00 16.87 1DLC1530 ATOM 1407 C THR 236 36.816 59.809 46.545 1.00 16.35 1DLC1531 ATOM 1408 O THR 236 36.196 58.763 46.418 1.00 16.83 1DLC1532 ATOM 1409 CB THR 236 39.284 59.705 46.966 1.00 15.64 1DLC1533 ATOM 1410 OG1 THR 236 40.562 59.726 46.323 1.00 21.58 1DLC1534 ATOM 1411 CG2 THR 236 39.073 58.337 47.618 1.00 11.02 1DLC1535 ATOM 1412 N GLN 237 36.333 60.845 47.216 1.00 16.17 1DLC1536 ATOM 1413 CA GLN 237 35.014 60.821 47.830 1.00 15.51 1DLC1537 ATOM 1414 C GLN 237 33.905 60.798 46.748 1.00 17.21 1DLC1538 ATOM 1415 O GLN 237 33.015 59.944 46.773 1.00 16.26 1DLC1539 ATOM 1416 CB GLN 237 34.881 62.037 48.751 1.00 16.03 1DLC1540 ATOM 1417 CG GLN 237 33.537 62.217 49.423 1.00 21.22 1DLC1541 ATOM 1418 CD GLN 237 32.598 63.054 48.596 1.00 25.16 1DLC1542 ATOM 1419 OE1 GLN 237 32.760 64.265 48.486 1.00 27.94 1DLC1543 ATOM 1420 NE2 GLN 237 31.633 62.411 47.969 1.00 27.25 1DLC1544 ATOM 1421 N GLU 238 33.998 61.704 45.776 1.00 18.54 1DLC1545 ATOM 1422 CA GLU 238 33.016 61.807 44.693 1.00 19.10 1DLC1546 ATOM 1423 C GLU 238 32.901 60.561 43.828 1.00 19.60 1DLC1547 ATOM 1424 O GLU 238 31.802 60.063 43.584 1.00 22.82 1DLC1548 ATOM 1425 CB GLU 238 33.326 63.001 43.789 1.00 20.79 1DLC1549 ATOM 1426 CG GLU 238 33.126 64.348 44.446 1.00 32.20 1DLC1550 ATOM 1427 CD GLU 238 33.403 65.518 43.513 1.00 38.00 1DLC1551 ATOM 1428 OE1 GLU 238 33.582 65.314 42.283 1.00 38.36 1DLC1552 ATOM 1429 OE2 GLU 238 33.434 66.657 44.028 1.00 45.77 1DLC1553 ATOM 1430 N TYR 239 34.032 60.082 43.328 1.00 17.99 1DLC1554 ATOM 1431 CA TYR 239 34.041 58.899 42.481 1.00 16.20 1DLC1555 ATOM 1432 C TYR 239 33.495 57.670 43.212 1.00 15.23 1DLC1556 ATOM 1433 O TYR 239 32.726 56.900 42.652 1.00 15.80 1DLC1557 ATOM 1434 CB TYR 239 35.455 58.646 41.965 1.00 18.91 1DLC1558 ATOM 1435 CG TYR 239 35.987 59.715 41.022 1.00 15.91 1DLC1559 ATOM 1436 CD1 TYR 239 35.124 60.541 40.304 1.00 14.94 1DLC1560 ATOM 1437 CD2 TYR 239 37.357 59.844 40.794 1.00 18.81 1DLC1561 ATOM 1438 CE1 TYR 239 35.612 61.455 39.375 1.00 12.13 1DLC1562 ATOM 1439 CE2 TYR 239 37.853 60.756 39.863 1.00 15.85 1DLC1563 ATOM 1440 CZ TYR 239 36.978 61.552 39.155 1.00 13.69 1DLC1564 ATOM 1441 OH TYR 239 37.468 62.392 38.181 1.00 16.58 1DLC1565 ATOM 1442 N THR 240 33.849 57.529 44.486 1.00 17.13 1DLC1566 ATOM 1443 CA THR 240 33.385 56.406 45.296 1.00 14.37 1DLC1567 ATOM 1444 C THR 240 31.878 56.494 45.457 1.00 16.34 1DLC1568 ATOM 1445 O THR 240 31.155 55.554 45.126 1.00 17.60 1DLC1569 ATOM 1446 CB THR 240 34.041 56.398 46.701 1.00 17.40 1DLC1570 ATOM 1447 OG1 THR 240 35.450 56.166 46.573 1.00 22.45 1DLC1571 ATOM 1448 CG2 THR 240 33.436 55.308 47.585 1.00 14.03 1DLC1572 ATOM 1449 N ASP 241 31.406 57.637 45.946 1.00 16.35 1DLC1573 ATOM 1450 CA ASP 241 29.977 57.844 46.145 1.00 13.45 1DLC1574 ATOM 1451 C ASP 241 29.170 57.692 44.863 1.00 15.38 1DLC1575 ATOM 1452 O ASP 241 28.119 57.051 44.862 1.00 21.27 1DLC1576 ATOM 1453 CB ASP 241 29.709 59.192 46.813 1.00 12.03 1DLC1577 ATOM 1454 CG ASP 241 30.062 59.192 48.290 1.00 10.13 1DLC1578 ATOM 1455 OD1 ASP 241 30.272 58.107 48.864 1.00 15.38 1DLC1579 ATOM 1456 OD2 ASP 241 30.122 60.277 48.890 1.00 14.27 1DLC1580 ATOM 1457 N HIS 242 29.692 58.205 43.757 1.00 14.94 1DLC1581 ATOM 1458 CA HIS 242 28.996 58.082 42.487 1.00 15.39 1DLC1582 ATOM 1459 C HIS 242 28.766 56.608 42.139 1.00 17.79 1DLC1583 ATOM 1460 O HIS 242 27.659 56.214 41.793 1.00 22.62 1DLC1584 ATOM 1461 CB HIS 242 29.781 58.772 41.360 1.00 15.91 1DLC1585 ATOM 1462 CG HIS 242 29.170 58.600 39.997 1.00 17.44 1DLC1586 ATOM 1463 ND1 HIS 242 28.285 59.508 39.454 1.00 20.18 1DLC1587 ATOM 1464 CD2 HIS 242 29.320 57.623 39.069 1.00 17.90 1DLC1588 ATOM 1465 CE1 HIS 242 27.916 59.100 38.251 1.00 16.84 1DLC1589 ATOM 1466 NE2 HIS 242 28.530 57.958 37.995 1.00 20.33 1DLC1590 ATOM 1467 N CYS 243 29.804 55.793 42.262 1.00 17.39 1DLC1591 ATOM 1468 CA CYS 243 29.694 54.377 41.924 1.00 17.86 1DLC1592 ATOM 1469 C CYS 243 28.721 53.588 42.776 1.00 17.12 1DLC1593 ATOM 1470 O CYS 243 27.939 52.800 42.251 1.00 21.15 1DLC1594 ATOM 1471 CB CYS 243 31.071 53.712 41.923 1.00 15.41 1DLC1595 ATOM 1472 SG CYS 243 32.126 54.356 40.620 1.00 18.63 1DLC1596 ATOM 1473 N VAL 244 28.742 53.812 44.083 1.00 17.77 1DLC1597 ATOM 1474 CA VAL 244 27.829 53.099 44.961 1.00 17.07 1DLC1598 ATOM 1475 C VAL 244 26.368 53.507 44.693 1.00 17.91 1DLC1599 ATOM 1476 O VAL 244 25.492 52.658 44.569 1.00 17.98 1DLC1600 ATOM 1477 CB VAL 244 28.185 53.318 46.434 1.00 16.68 1DLC1601 ATOM 1478 CG1 VAL 244 27.179 52.611 47.319 1.00 15.45 1DLC1602 ATOM 1479 CG2 VAL 244 29.582 52.804 46.711 1.00 11.35 1DLC1603 ATOM 1480 N LYS 245 26.129 54.805 44.551 1.00 19.29 1DLC1604 ATOM 1481 CA LYS 245 24.788 55.326 44.282 1.00 21.04 1DLC1605 ATOM 1482 C LYS 245 24.142 54.667 43.056 1.00 23.00 1DLC1606 ATOM 1483 O LYS 245 23.031 54.139 43.137 1.00 24.89 1DLC1607 ATOM 1484 CB LYS 245 24.855 56.837 44.073 1.00 21.68 1DLC1608 ATOM 1485 CG LYS 245 23.552 57.472 43.640 1.00 22.74 1DLC1609 ATOM 1486 CD LYS 245 23.779 58.929 43.268 1.00 30.91 1DLC1610 ATOM 1487 CE LYS 245 22.469 59.687 43.068 1.00 34.31 1DLC1611 ATOM 1488 NZ LYS 245 21.742 59.275 41.844 1.00 37.08 1DLC1612 ATOM 1489 N TRP 246 24.848 54.682 41.930 1.00 20.59 1DLC1613 ATOM 1490 CA TRP 246 24.332 54.088 40.701 1.00 19.32 1DLC1614 ATOM 1491 C TRP 246 24.386 52.568 40.685 1.00 21.56 1DLC1615 ATOM 1492 O TRP 246 23.604 51.918 39.983 1.00 23.26 1DLC1616 ATOM 1493 CB TRP 246 25.026 54.695 39.489 1.00 16.97 1DLC1617 ATOM 1494 CG TRP 246 24.705 56.132 39.400 1.00 20.83 1DLC1618 ATOM 1495 CD1 TRP 246 25.528 57.179 39.697 1.00 22.17 1DLC1619 ATOM 1496 CD2 TRP 246 23.427 56.697 39.096 1.00 21.29 1DLC1620 ATOM 1497 NE1 TRP 246 24.837 58.361 39.609 1.00 24.09 1DLC1621 ATOM 1498 CE2 TRP 246 23.546 58.097 39.239 1.00 23.54 1DLC1622 ATOM 1499 CE3 TRP 246 22.191 56.157 38.722 1.00 20.29 1DLC1623 ATOM 1500 CZ2 TRP 246 22.473 58.966 39.021 1.00 23.70 1DLC1624 ATOM 1501 CZ3 TRP 246 21.127 57.017 38.507 1.00 22.34 1DLC1625 ATOM 1502 CH2 TRP 246 21.274 58.410 38.657 1.00 23.62 1DLC1626 ATOM 1503 N TYR 247 25.304 51.997 41.460 1.00 20.03 1DLC1627 ATOM 1504 CA TYR 247 25.385 50.549 41.558 1.00 20.17 1DLC1628 ATOM 1505 C TYR 247 24.034 50.088 42.133 1.00 19.37 1DLC1629 ATOM 1506 O TYR 247 23.360 49.230 41.561 1.00 19.35 1DLC1630 ATOM 1507 CB TYR 247 26.528 50.121 42.494 1.00 17.68 1DLC1631 ATOM 1508 CG TYR 247 26.392 48.689 42.957 1.00 13.41 1DLC1632 ATOM 1509 CD1 TYR 247 26.579 47.633 42.067 1.00 14.48 1DLC1633 ATOM 1510 CD2 TYR 247 25.966 48.398 44.247 1.00 11.29 1DLC1634 ATOM 1511 CE1 TYR 247 26.331 46.325 42.446 1.00 14.18 1DLC1635 ATOM 1512 CE2 TYR 247 25.714 47.096 44.637 1.00 13.99 1DLC1636 ATOM 1513 CZ TYR 247 25.892 46.063 43.729 1.00 16.05 1DLC1637 ATOM 1514 OH TYR 247 25.586 44.773 44.087 1.00 19.99 1DLC1638 ATOM 1515 N ASN 248 23.634 50.709 43.243 1.00 16.91 1DLC1639 ATOM 1516 CA ASN 248 22.373 50.393 43.905 1.00 19.32 1DLC1640 ATOM 1517 C ASN 248 21.147 50.687 43.031 1.00 19.33 1DLC1641 ATOM 1518 O ASN 248 20.169 49.939 43.050 1.00 18.74 1DLC1642 ATOM 1519 CB ASN 248 22.276 51.116 45.250 1.00 18.47 1DLC1643 ATOM 1520 CG ASN 248 23.141 50.471 46.315 1.00 23.56 1DLC1644 ATOM 1521 OD1 ASN 248 23.184 49.249 46.438 1.00 28.32 1DLC1645 ATOM 1522 ND2 ASN 248 23.844 51.284 47.081 1.00 24.45 1DLC1646 ATOM 1523 N VAL 249 21.207 51.763 42.253 1.00 17.79 1DLC1647 ATOM 1524 CA VAL 249 20.105 52.103 41.366 1.00 16.98 1DLC1648 ATOM 1525 C VAL 249 19.883 50.921 40.422 1.00 19.97 1DLC1649 ATOM 1526 O VAL 249 18.763 50.425 40.284 1.00 22.20 1DLC1650 ATOM 1527 CB VAL 249 20.403 53.384 40.550 1.00 15.18 1DLC1651 ATOM 1528 CG1 VAL 249 19.374 53.566 39.445 1.00 8.38 1DLC1652 ATOM 1529 CG2 VAL 249 20.399 54.596 41.467 1.00 12.81 1DLC1653 ATOM 1530 N GLY 250 20.970 50.431 39.834 1.00 19.71 1DLC1654 ATOM 1531 CA GLY 250 20.879 49.304 38.924 1.00 20.85 1DLC1655 ATOM 1532 C GLY 250 20.409 48.035 39.609 1.00 22.20 1DLC1656 ATOM 1533 O GLY 250 19.558 47.316 39.089 1.00 26.29 1DLC1657 ATOM 1534 N LEU 251 20.935 47.772 40.797 1.00 20.95 1DLC1658 ATOM 1535 CA LEU 251 20.554 46.594 41.563 1.00 20.76 1DLC1659 ATOM 1536 C LEU 251 19.031 46.532 41.792 1.00 22.33 1DLC1660 ATOM 1537 O LEU 251 18.386 45.516 41.502 1.00 21.83 1DLC1661 ATOM 1538 CB LEU 251 21.299 46.597 42.900 1.00 17.68 1DLC1662 ATOM 1539 CG LEU 251 21.274 45.306 43.716 1.00 19.56 1DLC1663 ATOM 1540 CD1 LEU 251 21.908 44.160 42.937 1.00 16.74 1DLC1664 ATOM 1541 CD2 LEU 251 22.002 45.537 45.009 1.00 16.93 1DLC1665 ATOM 1542 N ASP 252 18.463 47.629 42.287 1.00 25.34 1DLC1666 ATOM 1543 CA ASP 252 17.023 47.721 42.548 1.00 26.45 1DLC1667 ATOM 1544 C ASP 252 16.172 47.589 41.288 1.00 29.16 1DLC1668 ATOM 1545 O ASP 252 15.089 47.015 41.322 1.00 32.76 1DLC1669 ATOM 1546 CB ASP 252 16.684 49.029 43.257 1.00 28.64 1DLC1670 ATOM 1547 CG ASP 252 17.192 49.071 44.686 1.00 35.67 1DLC1671 ATOM 1548 OD1 ASP 252 17.305 48.002 45.331 1.00 40.98 1DLC1672 ATOM 1549 OD2 ASP 252 17.476 50.184 45.170 1.00 42.32 1DLC1673 ATOM 1550 N LYS 253 16.673 48.100 40.173 1.00 26.89 1DLC1674 ATOM 1551 CA LYS 253 15.953 48.009 38.916 1.00 27.76 1DLC1675 ATOM 1552 C LYS 253 15.801 46.549 38.449 1.00 27.94 1DLC1676 ATOM 1553 O LYS 253 14.893 46.226 37.692 1.00 33.46 1DLC1677 ATOM 1554 CB LYS 253 16.664 48.854 37.854 1.00 31.20 1DLC1678 ATOM 1555 CG LYS 253 15.927 48.957 36.523 1.00 41.11 1DLC1679 ATOM 1556 CD LYS 253 16.574 49.982 35.592 1.00 49.37 1DLC1680 ATOM 1557 CE LYS 253 16.569 51.381 36.206 1.00 55.35 1DLC1681 ATOM 1558 NZ LYS 253 17.234 52.399 35.335 1.00 58.91 1DLC1682 ATOM 1559 N LEU 254 16.674 45.662 38.915 1.00 26.78 1DLC1683 ATOM 1560 CA LEU 254 16.619 44.251 38.521 1.00 24.25 1DLC1684 ATOM 1561 C LEU 254 15.876 43.317 39.487 1.00 25.28 1DLC1685 ATOM 1562 O LEU 254 15.695 42.129 39.197 1.00 24.46 1DLC1686 ATOM 1563 CB LEU 254 18.027 43.713 38.289 1.00 22.43 1DLC1687 ATOM 1564 CG LEU 254 18.834 44.386 37.191 1.00 21.13 1DLC1688 ATOM 1565 CD1 LEU 254 20.199 43.748 37.114 1.00 19.25 1DLC1689 ATOM 1566 CD2 LEU 254 18.114 44.247 35.875 1.00 18.91 1DLC1690 ATOM 1567 N ARG 255 15.460 43.837 40.634 1.00 24.30 1DLC1691 ATOM 1568 CA ARG 255 14.738 43.018 41.598 1.00 26.66 1DLC1692 ATOM 1569 C ARG 255 13.400 42.587 41.003 1.00 26.42 1DLC1693 ATOM 1570 O ARG 255 12.638 43.406 40.497 1.00 28.64 1DLC1694 ATOM 1571 CB ARG 255 14.494 43.782 42.893 1.00 27.60 1DLC1695 ATOM 1572 CG ARG 255 15.646 44.655 43.323 1.00 35.20 1DLC1696 ATOM 1573 CD ARG 255 15.438 45.138 44.737 1.00 35.77 1DLC1697 ATOM 1574 NE ARG 255 15.670 44.042 45.666 1.00 40.94 1DLC1698 ATOM 1575 CZ ARG 255 16.779 43.903 46.381 1.00 41.53 1DLC1699 ATOM 1576 NH1 ARG 255 17.749 44.804 46.279 1.00 43.27 1DLC1700 ATOM 1577 NH2 ARG 255 16.940 42.839 47.153 1.00 41.04 1DLC1701 ATOM 1578 N GLY 256 13.132 41.291 41.043 1.00 25.67 1DLC1702 ATOM 1579 CA GLY 256 11.893 40.777 40.502 1.00 21.48 1DLC1703 ATOM 1580 C GLY 256 11.314 39.735 41.428 1.00 22.34 1DLC1704 ATOM 1581 O GLY 256 11.690 39.653 42.600 1.00 22.71 1DLC1705 ATOM 1582 N SER 257 10.401 38.927 40.907 1.00 22.70 1DLC1706 ATOM 1583 CA SER 257 9.766 37.885 41.708 1.00 22.19 1DLC1707 ATOM 1584 C SER 257 10.123 36.504 41.191 1.00 19.96 1DLC1708 ATOM 1585 O SER 257 10.073 35.527 41.928 1.00 22.04 1DLC1709 ATOM 1586 CB SER 257 8.240 38.045 41.690 1.00 22.99 1DLC1710 ATOM 1587 OG SER 257 7.714 37.784 40.395 1.00 26.85 1DLC1711 ATOM 1588 N SER 258 10.488 36.427 39.920 1.00 18.79 1DLC1712 ATOM 1589 CA SER 258 10.835 35.154 39.311 1.00 20.57 1DLC1713 ATOM 1590 C SER 258 12.277 34.694 39.511 1.00 22.33 1DLC1714 ATOM 1591 O SER 258 13.156 35.462 39.895 1.00 24.89 1DLC1715 ATOM 1592 CB SER 258 10.544 35.191 37.809 1.00 19.52 1DLC1716 ATOM 1593 OG SER 258 11.502 35.975 37.113 1.00 24.21 1DLC1717 ATOM 1594 N TYR 259 12.494 33.419 39.212 1.00 22.78 1DLC1718 ATOM 1595 CA TYR 259 13.799 32.787 39.281 1.00 23.11 1DLC1719 ATOM 1596 C TYR 259 14.714 33.449 38.243 1.00 25.26 1DLC1720 ATOM 1597 O TYR 259 15.901 33.677 38.490 1.00 26.66 1DLC1721 ATOM 1598 CB TYR 259 13.655 31.300 38.953 1.00 21.44 1DLC1722 ATOM 1599 CG TYR 259 14.959 30.627 38.663 1.00 21.31 1DLC1723 ATOM 1600 CD1 TYR 259 15.812 30.253 39.698 1.00 22.67 1DLC1724 ATOM 1601 CD2 TYR 259 15.369 30.411 37.351 1.00 19.37 1DLC1725 ATOM 1602 CE1 TYR 259 17.045 29.682 39.432 1.00 23.31 1DLC1726 ATOM 1603 CE2 TYR 259 16.592 29.847 37.078 1.00 21.89 1DLC1727 ATOM 1604 CZ TYR 259 17.430 29.485 38.121 1.00 21.29 1DLC1728 ATOM 1605 OH TYR 259 18.655 28.932 37.850 1.00 26.88 1DLC1729 ATOM 1606 N GLU 260 14.154 33.732 37.073 1.00 21.58 1DLC1730 ATOM 1607 CA GLU 260 14.900 34.374 36.001 1.00 21.56 1DLC1731 ATOM 1608 C GLU 260 15.315 35.785 36.432 1.00 24.51 1DLC1732 ATOM 1609 O GLU 260 16.393 36.262 36.075 1.00 27.27 1DLC1733 ATOM 1610 CB GLU 260 14.064 34.432 34.723 1.00 20.53 1DLC1734 ATOM 1611 CG GLU 260 13.701 33.066 34.117 1.00 20.94 1DLC1735 ATOM 1612 CD GLU 260 12.625 32.287 34.887 1.00 23.83 1DLC1736 ATOM 1613 OE1 GLU 260 11.805 32.886 35.616 1.00 27.07 1DLC1737 ATOM 1614 OE2 GLU 260 12.593 31.051 34.743 1.00 26.90 1DLC1738 ATOM 1615 N SER 261 14.472 36.439 37.226 1.00 22.78 1DLC1739 ATOM 1616 CA SER 261 14.792 37.777 37.716 1.00 24.00 1DLC1740 ATOM 1617 C SER 261 16.020 37.733 38.617 1.00 22.53 1DLC1741 ATOM 1618 O SER 261 16.941 38.550 38.490 1.00 21.49 1DLC1742 ATOM 1619 CB SER 261 13.632 38.361 38.516 1.00 25.06 1DLC1743 ATOM 1620 OG SER 261 12.581 38.742 37.657 1.00 40.53 1DLC1744 ATOM 1621 N TRP 262 16.017 36.775 39.534 1.00 17.09 1DLC1745 ATOM 1622 CA TRP 262 17.125 36.627 40.450 1.00 19.88 1DLC1746 ATOM 1623 C TRP 262 18.464 36.308 39.710 1.00 18.85 1DLC1747 ATOM 1624 O TRP 262 19.496 36.795 40.213 1.00 22.45 1DLC1748 ATOM 1625 CB TRP 262 16.812 35.590 41.518 1.00 16.11 1DLC1749 ATOM 1626 CG TRP 262 17.835 35.588 42.585 1.00 17.10 1DLC1750 ATOM 1627 CD1 TRP 262 17.807 36.307 43.745 1.00 17.25 1DLC1751 ATOM 1628 CD2 TRP 262 19.065 34.852 42.593 1.00 17.80 1DLC1752 ATOM 1629 NE1 TRP 262 18.943 36.061 44.476 1.00 18.81 1DLC1753 ATOM 1630 CE2 TRP 262 19.735 35.175 43.794 1.00 18.51 1DLC1754 ATOM 1631 CE3 TRP 262 19.668 33.951 41.699 1.00 15.16 1DLC1755 ATOM 1632 CZ2 TRP 262 20.982 34.626 44.130 1.00 21.00 1DLC1756 ATOM 1633 CZ3 TRP 262 20.906 33.406 42.029 1.00 15.42 1DLC1757 ATOM 1634 CH2 TRP 262 21.550 33.745 43.235 1.00 19.20 1DLC1758 ATOM 1635 N VAL 263 18.458 35.502 38.709 1.00 19.89 1DLC1759 ATOM 1636 CA VAL 263 19.708 35.174 38.014 1.00 18.35 1DLC1760 ATOM 1637 C VAL 263 20.311 36.456 37.453 1.00 20.15 1DLC1761 ATOM 1638 O VAL 263 21.505 36.7d9 37.632 1.00 24.22 1DLC1762 ATOM 1639 CB VAL 263 19.528 34.097 36.887 1.00 18.77 1DLC1763 ATOM 1640 CG1 VAL 263 20.859 33.850 36.151 1.00 12.43 1DLC1764 ATOM 1641 CG2 VAL 263 19.042 32.778 37.488 1.00 14.72 1DLC1765 ATOM 1642 N ASN 264 19.474 37.289 36.838 1.00 19.11 1DLC1766 ATOM 1643 CA ASN 264 19.924 38.567 36.287 1.00 19.35 1DLC1767 ATOM 1644 C ASN 264 20.437 39.485 37.390 1.00 19.34 1DLC1768 ATOM 1645 O ASN 264 21.531 40.031 37.307 1.00 21.96 1DLC1769 ATOM 1646 CB ASN 264 18.784 39.256 35.563 1.00 24.05 1DLC1770 ATOM 1647 CG ASN 264 18.415 38.557 34.294 1.00 30.20 1DLC1771 ATOM 1648 OD1 ASN 264 19.233 37.850 33.710 1.00 35.20 1DLC1772 ATOM 1649 ND2 ASN 264 17.179 38.734 33.855 1.00 30.82 1DLC1773 ATOM 1650 N PHE 265 19.629 39.631 38.429 1.00 19.08 1DLC1774 ATOM 1651 CA PHE 265 19.941 40.445 39.594 1.00 16.55 1DLC1775 ATOM 1652 C PHE 265 21.318 40.065 40.165 1.00 17.77 1DLC1776 ATOM 1653 O PHE 265 22.194 40.914 40.321 1.00 19.27 1DLC1777 ATOM 1654 CB PHE 265 18.821 40.223 40.619 1.00 12.97 1DLC1778 ATOM 1655 CG PHE 265 19.066 40.831 41.971 1.00 10.89 1DLC1779 ATOM 1656 CD1 PHE 265 18.677 42.137 42.241 1.00 13.68 1DLC1780 ATOM 1657 CD2 PHE 265 19.574 40.059 43.010 1.00 9.55 1DLC1781 ATOM 1658 CE1 PHE 265 18.780 42.663 43.530 1.00 12.86 1DLC1782 ATOM 1659 CE2 PHE 265 19.680 40.571 44.295 1.00 10.43 1DLC1783 ATOM 1660 CZ PHE 265 19.281 41.876 44.559 1.00 10.95 1DLC1784 ATOM 1661 N ASN 266 21.518 38.773 40.403 1.00 19.03 1DLC1785 ATOM 1662 CA ASN 266 22.766 38.265 40.954 1.00 17.33 1DLC1786 ATOM 1663 C ASN 266 23.957 38.336 39.992 1.00 17.92 1DLC1787 ATOM 1664 O ASN 266 25.092 38.493 40.435 1.00 22.09 1DLC1788 ATOM 1665 CB ASN 266 22.584 36.840 41.468 1.00 15.11 1DLC1789 ATOM 1666 CG ASN 266 23.826 36.313 42.142 1.00 17.39 1DLC1790 ATOM 1667 OD1 ASN 266 24.244 36.822 43.181 1.00 17.95 1DLC1791 ATOM 1668 ND2 ASN 266 24.444 35.307 41.543 1.00 18.20 1DLC1792 ATOM 1669 N ARG 267 23.716 38.190 38.692 1.00 17.41 1DLC1793 ATOM 1670 CA ARG 267 24.801 38.283 37.707 1.00 17.83 1DLC1794 ATOM 1671 C ARG 267 25.306 39.730 37.662 1.00 19.29 1DLC1795 ATOM 1672 O ARG 267 26.505 39.976 37.578 1.00 20.96 1DLC1796 ATOM 1673 CB ARG 267 24.321 37.849 36.322 1.00 16.99 1DLC1797 ATOM 1674 CG ARG 267 25.377 37.917 35.248 1.00 17.92 1DLC1798 ATOM 1675 CD ARG 267 24.824 37.461 33.916 1.00 22.41 1DLC1799 ATOM 1676 NE ARG 267 24.427 36.052 33.942 1.00 35.91 1DLC1800 ATOM 1677 CZ ARG 267 23.190 35.599 33.727 1.00 41.26 1DLC1801 ATOM 1678 NH1 ARG 267 22.183 36.431 33.464 1.00 42.55 1DLC1802 ATOM 1679 NH2 ARG 267 22.959 34.293 33.767 1.00 44.18 1DLC1803 ATOM 1680 N TYR 268 24.378 40.681 37.735 1.00 17.33 1DLC1804 ATOM 1681 CA TYR 268 24.711 42.098 37.748 1.00 15.33 1DLC1805 ATOM 1682 C TYR 268 25.505 42.391 39.018 1.00 17.40 1DLC1806 ATOM 1683 O TYR 268 26.557 43.032 38.976 1.00 20.28 1DLC1807 ATOM 1684 CB TYR 268 23.432 42.932 37.739 1.00 13.81 1DLC1808 ATOM 1685 CG TYR 268 23.625 44.400 38.058 1.00 15.29 1DLC1809 ATOM 1686 CD1 TYR 268 23.588 44.852 39.378 1.00 17.01 1DLC1810 ATOM 1687 CD2 TYR 268 23.808 45.344 37.042 1.00 12.55 1DLC1811 ATOM 1688 CE1 TYR 268 23.720 46.207 39.685 1.00 18.91 1DLC1812 ATOM 1689 CE2 TYR 268 23.937 46.703 37.335 1.00 15.35 1DLC1813 ATOM 1690 CZ TYR 268 23.891 47.129 38.664 1.00 17.81 1DLC1814 ATOM 1691 OH TYR 268 23.989 48.470 38.983 1.00 14.63 1DLC1815 ATOM 1692 N ARG 269 24.982 41.936 40.152 1.00 15.99 1DLC1816 ATOM 1693 CA ARG 269 25.643 42.129 41.436 1.00 16.03 1DLC1817 ATOM 1694 C ARG 269 27.084 41.570 41.420 1.00 20.77 1DLC1818 ATOM 1695 O ARG 269 28.024 42.257 41.831 1.00 23.24 1DLC1819 ATOM 1696 CB ARG 269 24.815 41.485 42.538 1.00 11.54 1DLC1820 ATOM 1697 CG ARG 269 25.506 41.407 43.864 1.00 10.15 1DLC1821 ATOM 1698 CD ARG 269 25.030 40.181 44.571 1.00 14.41 1DLC1822 ATOM 1699 NE ARG 269 23.862 40.441 45.396 1.00 17.34 1DLC1823 ATOM 1700 CZ ARG 269 22.933 39.541 45.710 1.00 21.53 1DLC1824 ATOM 1701 NH1 ARG 269 22.991 38.292 45.259 1.00 20.03 1DLC1825 ATOM 1702 NH2 ARG 269 21.977 39.878 46.558 1.00 26.32 1DLC1826 ATOM 1703 N ARG 270 27.263 40.350 40.907 1.00 20.00 1DLC1827 ATOM 1704 CA ARG 270 28.592 39.749 40.821 1.00 19.69 1DLC1828 ATOM 1705 C ARG 270 29.517 40.503 39.850 1.00 19.79 1DLC1829 ATOM 1706 O ARG 270 30.647 40.841 40.199 1.00 23.48 1DLC1830 ATOM 1707 CB ARG 270 28.509 38.285 40.386 1.00 21.51 1DLC1831 ATOM 1708 CG ARG 270 29.863 37.543 40.405 1.00 22.79 1DLC1832 ATOM 1709 CD ARG 270 29.949 36.544 39.258 1.00 23.46 1DLC1833 ATOM 1710 NE ARG 270 28.710 35.781 39.194 1.00 27.60 1DLC1834 ATOM 1711 CZ ARG 270 28.020 35.535 38.087 1.00 23.27 1DLC1835 ATOM 1712 NH1 ARG 270 28.437 35.961 36.906 1.00 16.76 1DLC1836 ATOM 1713 NH2 ARG 270 26.852 34.934 38.189 1.00 27.70 1DLC1837 ATOM 1714 N GLU 271 29.044 40.782 38.641 1.00 16.09 1DLC1838 ATOM 1715 CA GLU 271 29.871 41.489 37.672 1.00 16.33 1DLC1839 ATOM 1716 C GLU 271 30.236 42.910 38.103 1.00 19.12 1DLC1840 ATOM 1717 O GLU 271 31.364 43.351 37.878 1.00 22.66 1DLC1841 ATOM 1718 CB GLU 271 29.229 41.471 36.285 1.00 14.28 1DLC1842 ATOM 1719 CG GLU 271 29.077 40.055 35.742 1.00 18.54 1DLC1843 ATOM 1720 CD GLU 271 28.846 39.984 34.242 1.00 22.46 1DLC1844 ATOM 1721 OE1 GLU 271 28.930 41.022 33.548 1.00 28.08 1DLC1845 ATOM 1722 OE2 GLU 271 28.597 38.869 33.744 1.00 24.80 1DLC1846 ATOM 1723 N MET 272 29.305 43.616 38.745 1.00 17.93 1DLC1847 ATOM 1724 CA MET 272 29.580 44.968 39.223 1.00 15.97 1DLC1848 ATOM 1725 C MET 272 30.544 44.914 40.405 1.00 16.81 1DLC1849 ATOM 1726 O MET 272 31.253 45.876 40.684 1.00 20.74 1DLC1850 ATOM 1727 CB MET 272 28.300 45.705 39.616 1.00 14.65 1DLC1851 ATOM 1728 CG MET 272 27.362 45.953 38.464 1.00 20.31 1DLC1852 ATOM 1729 SD MET 272 28.183 46.581 36.973 1.00 27.85 1DLC1853 ATOM 1730 CE MET 272 27.795 48.276 37.085 1.00 32.60 1DLC1854 ATOM 1731 N THR 273 30.571 43.789 41.104 1.00 14.53 1DLC1855 ATOM 1732 CA THR 273 31.491 43.631 42.220 1.00 16.38 1DLC1856 ATOM 1733 C THR 273 32.931 43.495 41.701 1.00 17.79 1DLC1857 ATOM 1734 O THR 273 33.835 44.207 42.142 1.00 19.00 1DLC1858 ATOM 1735 CB THR 273 31.130 42.402 43.072 1.00 13.43 1DLC1859 ATOM 1736 OG1 THR 273 29.875 42.632 43.716 1.00 13.76 1DLC1860 ATOM 1737 CG2 THR 273 32.190 42.146 44.139 1.00 12.75 1DLC1861 ATOM 1738 N LEU 274 33.108 42.634 40.702 1.00 18.60 1DLC1862 ATOM 1739 CA LEU 274 34.413 42.376 40.100 1.00 17.81 1DLC1863 ATOM 1740 C LEU 274 35.000 43.542 39.305 1.00 18.48 1DLC1864 ATOM 1741 O LEU 274 36.214 43.754 39.306 1.00 23.04 1DLC1865 ATOM 1742 CB LEU 274 34.340 41.136 39.198 1.00 10.87 1DLC1866 ATOM 1743 CG LEU 274 33.850 39.850 39.870 1.00 11.27 1DLC1867 ATOM 1744 CD1 LEU 274 33.801 38.730 38.867 1.00 10.38 1DLC1868 ATOM 1745 CD2 LEU 274 34.735 39.476 41.047 1.00 9.69 1DLC1869 ATOM 1746 N THR 275 34.143 44.300 38.632 1.00 16.36 1DLC1870 ATOM 1747 CA THR 275 34.611 45.412 37.813 1.00 16.92 1DLC1871 ATOM 1748 C THR 275 34.489 46.807 38.413 1.00 18.24 1DLC1872 ATOM 1749 O THR 275 35.169 47.734 37.967 1.00 22.33 1DLC1873 ATOM 1750 CB THR 275 33.932 45.417 36.421 1.00 16.38 1DLC1874 ATOM 1751 OG1 THR 275 32.508 45.523 36.581 1.00 22.03 1DLC1875 ATOM 1752 CG2 THR 275 34.259 44.148 35.663 1.00 13.77 1DLC1876 ATOM 1753 N VAL 276 33.626 46.972 39.410 1.00 17.04 1DLC1877 ATOM 1754 CA VAL 276 33.443 48.287 40.021 1.00 14.32 1DLC1878 ATOM 1755 C VAL 276 33.739 48.366 41.523 1.00 15.28 1DLC1879 ATOM 1756 O VAL 276 34.637 49.093 41.949 1.00 15.38 1DLC1880 ATOM 1757 CB VAL 276 32.008 48.832 39.749 1.00 14.77 1DLC1881 ATOM 1758 CG1 VAL 276 31.796 50.185 40.439 1.00 14.41 1DLC1882 ATOM 1759 CG2 VAL 276 31.764 48.963 38.250 1.00 10.22 1DLC1883 ATOM 1760 N LEU 277 33.005 47.585 42.311 1.00 17.20 1DLC1884 ATOM 1761 CA LEU 277 33.137 47.596 43.767 1.00 16.40 1DLC1885 ATOM 1762 C LEU 277 34.504 47.219 44.330 1.00 16.22 1DLC1886 ATOM 1763 O LEU 277 34.967 47.831 45.294 1.00 16.50 1DLC1887 ATOM 1764 CB LEU 277 32.009 46.781 44.421 1.00 13.32 1DLC1888 ATOM 1765 CG LEU 277 30.565 47.184 44.067 1.00 10.97 1DLC1889 ATOM 1766 CD1 LEU 277 29.609 46.395 44.928 1.00 10.44 1DLC1890 ATOM 1767 CD2 LEU 277 30.326 48.681 44.254 1.00 5.94 1DLC1891 ATOM 1768 N ASP 278 35.143 46.210 43.747 1.00 16.09 1DLC1892 ATOM 1769 CA ASP 278 36.484 45.792 44.188 1.00 17.29 1DLC1893 ATOM 1770 C ASP 278 37.503 46.892 43.892 1.00 17.61 1DLC1894 ATOM 1771 O ASP 278 38.430 47.134 44.659 1.00 20.19 1DLC1895 ATOM 1772 CB ASP 278 36.923 44.506 43.469 1.00 16.99 1DLC1896 ATOM 1773 CG ASP 278 36.247 43.269 44.015 1.00 15.27 1DLC1897 ATOM 1774 OD1 ASP 278 35.693 43.336 45.127 1.00 18.92 1DLC1898 ATOM 1775 OD2 ASP 278 36.270 42.229 43.336 1.00 18.16 1DLC1899 ATOM 1776 N LEU 279 37.281 47.579 42.778 1.00 20.55 1DLC1900 ATOM 1777 CA LEU 279 38.137 48.660 42.317 1.00 19.58 1DLC1901 ATOM 1778 C LEU 279 38.086 49.881 43.234 1.00 19.74 1DLC1902 ATOM 1779 O LEU 279 39.128 50.342 43.710 1.00 22.71 1DLC1903 ATOM 1780 CB LEU 279 37.734 49.052 40.893 1.00 17.72 1DLC1904 ATOM 1781 CG LEU 279 38.749 49.808 40.046 1.00 16.46 1DLC1905 ATOM 1782 CD1 LEU 279 40.052 49.031 40.000 1.00 14.94 1DLC1906 ATOM 1783 CD2 LEU 279 38.188 49.989 38.641 1.00 16.14 1DLC1907 ATOM 1784 N ILE 280 36.879 50.375 43.517 1.00 18.89 1DLC1908 ATOM 1785 CA ILE 280 36.719 51.560 44.366 1.00 13.41 1DLC1909 ATOM 1786 C ILE 280 37.199 51.324 45.798 1.00 13.89 1DLC1910 ATOM 1787 O ILE 280 37.507 52.267 46.526 1.00 13.40 1DLC1911 ATOM 1788 CB ILE 280 35.256 52.105 44.363 1.00 14.32 1DLC1912 ATOM 1789 CG1 ILE 280 34.321 51.163 45.122 1.00 13.32 1DLC1913 ATOM 1790 CG2 ILE 280 34.761 52.313 42.923 1.00 13.11 1DLC1914 ATOM 1791 CD1 ILE 280 32.919 51.689 45.250 1.00 13.97 1DLC1915 ATOM 1792 N ALA 281 37.279 50.057 46.190 1.00 14.85 1DLC1916 ATOM 1793 CA ALA 281 37.753 49.696 47.523 1.00 14.09 1DLC1917 ATOM 1794 C ALA 281 39.244 50.047 47.686 1.00 16.05 1DLC1918 ATOM 1795 O ALA 281 39.711 50.300 48.792 1.00 19.60 1DLC1919 ATOM 1796 CB ALA 281 37.534 48.218 47.758 1.00 10.28 1DLC1920 ATOM 1797 N LEU 282 39.968 50.109 46.568 1.00 17.34 1DLC1921 ATOM 1798 CA LEU 282 41.404 50.412 46.566 1.00 17.85 1DLC1922 ATOM 1799 C LEU 282 41.772 51.901 46.551 1.00 18.73 1DLC1923 ATOM 1800 O LEU 282 42.853 52.282 47.002 1.00 20.35 1DLC1924 ATOM 1801 CB LEU 282 42.088 49.692 45.396 1.00 13.56 1DLC1925 ATOM 1802 CG LEU 282 41.818 48.181 45.369 1.00 15.77 1DLC1926 ATOM 1803 CD1 LEU 282 42.557 47.527 44.222 1.00 15.69 1DLC1927 ATOM 1804 CD2 LEU 282 42.219 47.554 46.693 1.00 11.02 1DLC1928 ATOM 1805 N PHE 283 40.853 52.738 46.078 1.00 17.57 1DLC1929 ATOM 1806 CA PHE 283 41.056 54.189 45.993 1.00 16.08 1DLC1930 ATOM 1807 C PHE 283 41.766 54.859 47.190 1.00 17.36 1DLC1931 ATOM 1808 O PHE 283 42.711 55.622 47.003 1.00 18.59 1DLC1932 ATOM 1809 CB PHE 283 39.714 54.910 45.750 1.00 16.79 1DLC1933 ATOM 1810 CG PHE 283 39.107 54.676 44.384 1.00 11.95 1DLC1934 ATOM 1811 CD1 PHE 283 39.792 53.973 43.397 1.00 9.94 1DLC1935 ATOM 1812 CD2 PHE 283 37.851 55.199 44.083 1.00 11.93 1DLC1936 ATOM 1813 CE1 PHE 283 39.231 53.797 42.123 1.00 15.02 1DLC1937 ATOM 1814 CE2 PHE 283 37.284 55.027 42.815 1.00 13.95 1DLC1938 ATOM 1815 CZ PHE 283 37.978 54.325 41.832 1.00 8.45 1DLC1939 ATOM 1816 N PRO 284 41.325 54.577 48.432 1.00 16.44 1DLC1940 ATOM 1817 CA PRO 284 41.954 55.188 49.613 1.00 16.04 1DLC1941 ATOM 1818 C PRO 284 43.435 54.855 49.775 1.00 18.64 1DLC1942 ATOM 1819 O PRO 284 44.206 55.624 50.357 1.00 20.90 1DLC1943 ATOM 1820 CB PRO 284 41.154 54.593 50.771 1.00 11.65 1DLC1944 ATOM 1821 CG PRO 284 39.841 54.292 50.168 1.00 13.79 1DLC1945 ATOM 1822 CD PRO 284 40.210 53.707 48.843 1.00 14.01 1DLC1946 ATOM 1823 N LEU 285 43.825 53.697 49.263 1.00 19.68 1DLC1947 ATOM 1824 CA LEU 285 45.198 53.244 49.366 1.00 17.84 1DLC1948 ATOM 1825 C LEU 285 46.126 53.959 48.383 1.00 17.73 1DLC1949 ATOM 1826 O LEU 285 47.334 53.743 48.391 1.00 22.07 1DLC1950 ATOM 1827 CB LEU 285 45.248 51.719 49.220 1.00 19.70 1DLC1951 ATOM 1828 CG LEU 285 44.269 50.970 50.149 1.00 20.17 1DLC1952 ATOM 1829 CD1 LEU 285 44.337 49.484 49.897 1.00 22.11 1DLC1953 ATOM 1830 CD2 LEU 285 44.558 51.263 51.609 1.00 17.27 1DLC1954 ATOM 1831 N TYR 286 45.554 54.817 47.543 1.00 17.08 1DLC1955 ATOM 1832 CA TYR 286 46.335 55.608 46.588 1.00 16.87 1DLC1956 ATOM 1833 C TYR 286 46.878 56.856 47.292 1.00 17.31 1DLC1957 ATOM 1834 O TYR 286 47.635 57.630 46.709 1.00 18.04 1DLC1958 ATOM 1835 CB TYR 286 45.484 56.044 45.395 1.00 15.25 1DLC1959 ATOM 1836 CG TYR 286 44.982 54.917 44.529 1.00 17.75 1DLC1960 ATOM 1837 CD1 TYR 286 45.468 53.615 44.680 1.00 19.64 1DLC1961 ATOM 1838 CD2 TYR 286 44.008 55.149 43.559 1.00 19.56 1DLC1962 ATOM 1839 CE1 TYR 286 44.990 52.579 43.888 1.00 19.02 1DLC1963 ATOM 1840 CE2 TYR 286 43.526 54.121 42.763 1.00 17.69 1DLC1964 ATOM 1841 CZ TYR 286 44.016 52.846 42.933 1.00 17.71 1DLC1965 ATOM 1842 OH TYR 286 43.507 51.832 42.166 1.00 19.21 1DLC1966 ATOM 1843 N ASP 287 46.449 57.080 48.531 1.00 15.82 1DLC1967 ATOM 1844 CA ASP 287 46.942 58.221 49.279 1.00 15.74 1DLC1968 ATOM 1845 C ASP 287 48.293 57.856 49.888 1.00 15.59 1DLC1969 ATOM 1846 O ASP 287 48.376 57.359 51.013 1.00 15.25 1DLC1970 ATOM 1847 CB ASP 287 45.958 58.648 50.365 1.00 14.24 1DLC1971 ATOM 1848 CG ASP 287 46.307 60.007 50.970 1.00 19.57 1DLC1972 ATOM 1849 OD1 ASP 287 47.482 60.422 50.914 1.00 23.20 1DLC1973 ATOM 1850 OD2 ASP 287 45.405 60.672 51.519 1.00 24.37 1DLC1974 ATOM 1851 N VAL 288 49.352 58.154 49.142 1.00 17.00 1DLC1975 ATOM 1852 CA VAL 288 50.717 57.860 49.564 1.00 19.40 1DLC1976 ATOM 1853 C VAL 288 51.236 58.650 50.761 1.00 20.76 1DLC1977 ATOM 1854 O VAL 288 52.334 58.403 51.236 1.00 24.76 1DLC1978 ATOM 1855 CB VAL 288 51.702 57.989 48.397 1.00 17.31 1DLC1979 ATOM 1856 CG1 VAL 288 51.291 57.054 47.285 1.00 18.35 1DLC1980 ATOM 1857 CG2 VAL 288 51.762 59.418 47.905 1.00 17.23 1DLC1981 ATOM 1858 N ARG 289 50.447 59.598 51.248 1.00 23.06 1DLC1982 ATOM 1859 CA ARG 289 50.846 60.391 52.410 1.00 22.35 1DLC1983 ATOM 1860 C ARG 289 50.361 59.717 53.669 1.00 20.93 1DLC1984 ATOM 1861 O ARG 289 51.051 59.715 54.684 1.00 21.28 1DLC1985 ATOM 1862 CB ARG 289 50.283 61.800 52.311 1.00 28.20 1DLC1986 ATOM 1863 CG ARG 289 50.680 62.438 51.025 1.00 31.27 1DLC1987 ATOM 1864 CD ARG 289 50.447 63.905 51.004 1.00 41.78 1DLC1988 ATOM 1865 NE ARG 289 51.389 64.454 50.046 1.00 51.47 1DLC1989 ATOM 1866 CZ ARG 289 52.620 64.833 50.361 1.00 52.65 1DLC1990 ATOM 1867 NH1 ARG 289 53.034 64.743 51.621 1.00 52.33 1DLC1991 ATOM 1868 NH2 ARG 289 53.469 65.194 49.403 1.00 53.49 1DLC1992 ATOM 1869 N LEU 290 49.142 59.187 53.599 1.00 21.77 1DLC1993 ATOM 1870 CA LEU 290 48.535 58.454 54.710 1.00 19.60 1DLC1994 ATOM 1871 C LEU 290 49.127 57.042 54.690 1.00 19.04 1DLC1995 ATOM 1872 O LEU 290 49.307 56.414 55.728 1.00 16.89 1DLC1996 ATOM 1873 CB LEU 290 47.014 58.368 54.545 1.00 17.72 1DLC1997 ATOM 1874 CG LEU 290 46.117 59.392 55.235 1.00 17.03 1DLC1998 ATOM 1875 CD1 LEU 290 44.683 58.999 54.982 1.00 15.20 1DLC1999 ATOM 1876 CD2 LEU 290 46.382 59.429 56.728 1.00 13.88 1DLC2000 ATOM 1877 N TYR 291 49.429 56.555 53.490 1.00 17.26 1DLC2001 ATOM 1878 CA TYR 291 50.018 55.231 53.316 1.00 17.98 1DLC2002 ATOM 1879 C TYR 291 51.379 55.394 52.648 1.00 19.81 1DLC2003 ATOM 1880 O TYR 291 51.533 55.142 51.448 1.00 19.73 1DLC2004 ATOM 1881 CB TYR 291 49.092 54.352 52.475 1.00 16.70 1DLC2005 ATOM 1882 CG TYR 291 47.755 54.103 53.142 1.00 17.30 1DLC2006 ATOM 1883 CD1 TYR 291 47.582 53.028 54.024 1.00 15.12 1DLC2007 ATOM 1884 CD2 TYR 291 46.674 54.963 52.927 1.00 12.11 1DLC2008 ATOM 1885 CE1 TYR 291 46.379 52.820 54.672 1.00 15.98 1DLC2009 ATOM 1886 CE2 TYR 291 45.469 54.763 53.576 1.00 11.41 1DLC2010 ATOM 1887 CZ TYR 291 45.330 53.689 54.444 1.00 13.44 1DLC2011 ATOM 1888 OH TYR 291 44.140 53.472 55.077 1.00 16.97 1DLC2012 ATOM 1889 N PRO 292 52.383 55.841 53.428 1.00 18.71 1DLC2013 ATOM 1890 CA PRO 292 53.760 56.078 52.988 1.00 19.79 1DLC2014 ATOM 1891 C PRO 292 54.569 54.810 52.769 1.00 21.30 1DLC2015 ATOM 1892 O PRO 292 55.746 54.877 52.441 1.00 27.34 1DLC2016 ATOM 1893 CB PRO 292 54.351 56.913 54.127 1.00 20.00 1DLC2017 ATOM 1894 CG PRO 292 53.159 57.371 54.919 1.00 24.03 1DLC2018 ATOM 1895 CD PRO 292 52.248 56.202 54.843 1.00 17.48 1DLC2019 ATOM 1896 N LYS 293 53.959 53.657 53.010 1.00 20.08 1DLC2020 ATOM 1897 CA LYS 293 54.625 52.381 52.793 1.00 20.58 1DLC2021 ATOM 1898 C LYS 293 53.692 51.508 51.950 1.00 23.91 1DLC2022 ATOM 1899 O LYS 293 52.543 51.884 51.690 1.00 27.52 1DLC2023 ATOM 1900 CB LYS 293 54.881 51.655 54.114 1.00 17.96 1DLC2024 ATOM 1901 CG LYS 293 55.286 52.512 55.267 1.00 20.88 1DLC2025 ATOM 1902 CD LYS 293 55.560 51.644 56.484 1.00 25.87 1DLC2026 ATOM 1903 CE LYS 293 55.546 52.459 57.770 1.00 34.09 1DLC2027 ATOM 1904 NZ LYS 293 56.452 53.641 57.721 1.00 38.99 1DLC2028 ATOM 1905 N GLU 294 54.180 50.345 51.530 1.00 22.97 1DLC2029 ATOM 1906 CA GLU 294 53.359 49.411 50.772 1.00 20.92 1DLC2030 ATOM 1907 C GLU 294 52.267 48.916 51.722 1.00 20.22 1DLC2031 ATOM 1908 O GLU 294 52.471 48.835 52.938 1.00 19.74 1DLC2032 ATOM 1909 CB GLU 294 54.192 48.218 50.314 1.00 24.35 1DLC2033 ATOM 1910 CG GLU 294 55.435 48.586 49.521 1.00 36.21 1DLC2034 ATOM 1911 CD GLU 294 56.236 47.367 49.086 1.00 37.88 1DLC2035 ATOM 1912 OE1 GLU 294 56.648 46.574 49.966 1.00 43.62 1DLC2036 ATOM 1913 OE2 GLU 294 56.450 47.207 47.864 1.00 40.00 1DLC2037 ATOM 1914 N VAL 295 51.101 48.607 51.177 1.00 21.65 1DLC2038 ATOM 1915 CA VAL 295 49.999 48.127 52.002 1.00 21.78 1DLC2039 ATOM 1916 C VAL 295 49.628 46.669 51.752 1.00 20.58 1DLC2040 ATOM 1917 O VAL 295 49.519 46.236 50.608 1.00 21.08 SDLC2041 ATOM 1918 CB VAL 295 48.732 48.989 51.809 1.00 20.64 1DLC2042 ATOM 1919 CG1 VAL 295 47.553 48.390 52.569 1.00 22.03 1DLC2043 ATOM 1920 CG2 VAL 295 48.991 50.400 52.284 1.00 22.52 1DLC2044 ATOM 1921 N LYS 296 49.509 45.905 52.834 1.00 18.88 1DLC2045 ATOM 1922 CA LYS 296 49.082 44.516 52.754 1.00 17.81 1DLC2046 ATOM 1923 C LYS 296 47.586 44.560 53.085 1.00 20.39 1DLC2047 ATOM 1924 O LYS 296 47.195 45.013 54.172 1.00 20.26 1DLC2048 ATOM 1925 CB LYS 296 49.809 43.651 53.782 1.00 15.08 1DLC2049 ATOM 1926 CG LYS 296 49.313 42.216 53.816 1.00 12.45 1DLC2050 ATOM 1927 CD LYS 296 49.980 41.428 54.928 1.00 16.66 1DLC2051 ATOM 1928 CE LYS 296 49.434 40.008 55.028 1.00 12.92 1DLC2052 ATOM 1929 NZ LYS 296 48.362 39.892 56.047 1.00 15.35 1DLC2053 ATOM 1930 N THR 297 46.747 44.166 52.135 1.00 20.26 1DLC2054 ATOM 1931 CA THR 297 45.309 44.186 52.373 1.00 19.90 1DLC2055 ATOM 1932 C THR 297 44.572 43.049 51.671 1.00 19.99 1DLC2056 ATOM 1933 O THR 297 45.177 42.286 50.923 1.00 24.16 1DLC2057 ATOM 1934 CB THR 297 44.701 45.550 51.980 1.00 17.52 1DLC2058 ATOM 1935 OG1 THR 297 43.325 45.579 52.366 1.00 18.25 1DLC2059 ATOM 1936 CG2 THR 297 44.829 45.799 50.476 1.00 14.77 1DLC2060 ATOM 1937 N GLU 298 43.270 42.935 51.913 1.00 20.33 1DLC2061 ATOM 1938 CA GLU 298 42.461 41.874 51.307 1.00 19.29 1DLC2062 ATOM 1939 C GLU 298 40.997 42.259 51.106 1.00 17.75 1DLC2063 ATOM 1940 O GLU 298 40.470 43.129 51.795 1.00 20.54 1DLC2064 ATOM 1941 CB GLU 298 42.536 40.605 52.166 1.00 14.48 1DLC2065 ATOM 1942 CG GLU 298 42.130 40.827 53.611 1.00 14.45 1DLC2066 ATOM 1943 CD GLU 298 42.441 39.644 54.506 1.00 15.68 1DLC2067 ATOM 1944 OE1 GLU 298 43.588 39.157 54.490 1.00 22.29 1DLC2068 ATOM 1945 OE2 GLU 298 41.544 39.211 55.247 1.00 19.26 1DLC2069 ATOM 1946 N LEU 299 40.349 41.596 50.156 1.00 17.55 1DLC2070 ATOM 1947 CA LEU 299 38.933 41.826 49.856 1.00 18.90 1DLC2071 ATOM 1948 C LEU 299 38.165 40.652 50.488 1.00 21.39 1DLC2072 ATOM 1949 O LEU 299 38.385 39.493 50.108 1.00 23.60 1DLC2073 ATOM 1950 CB LEU 299 38.717 41.862 48.338 1.00 13.32 1DLC2074 ATOM 1951 CG LEU 299 39.472 42.945 47.563 1.00 10.97 1DLC2075 ATOM 1952 CD1 LEU 299 39.359 42.688 46.085 1.00 14.82 1DLC2076 ATOM 1953 CD2 LEU 299 38.929 44.312 47.894 1.00 9.97 1DLC2077 ATOM 1954 N THR 300 37.291 40.943 51.455 1.00 19.12 1DLC2078 ATOM 1955 CA THR 300 36.539 39.902 52.163 1.00 17.44 1DLC2079 ATOM 1956 C THR 300 35.105 39.598 51.710 1.00 20.09 1DLC2080 ATOM 1957 O THR 300 34.439 38.743 52.297 1.00 21.20 1DLC2081 ATOM 1958 CB THR 300 36.492 40.200 53.680 1.00 18.14 1DLC2082 ATOM 1959 OG1 THR 300 35.829 41.449 53.904 1.00 20.85 1DLC2083 ATOM 1960 CG2 THR 300 37.899 40.264 54.270 1.00 17.00 1DLC2084 ATOM 1961 N ARG 301 34.631 40.268 50.667 1.00 20.53 1DLC2085 ATOM 1962 CA ARG 301 33.259 40.074 50.184 1.00 18.35 1DLC2086 ATOM 1963 C ARG 301 32.963 38.762 49.451 1.00 19.18 1DLC2087 ATOM 1964 O ARG 301 33.850 38.158 48.849 1.00 18.71 1DLC2088 ATOM 1965 CB ARG 301 32.842 41.248 49.291 1.00 13.09 1DLC2089 ATOM 1966 CG ARG 301 33.280 41.126 47.830 1.00 13.61 1DLC2090 ATOM 1967 CD ARG 301 34.792 41.044 47.678 1.00 14.65 1DLC2091 ATOM 1968 NE ARG 301 35.197 40.844 46.291 1.00 14.20 1DLC2092 ATOM 1969 CZ ARG 301 35.305 39.661 45.690 1.00 17.27 1DLC2093 ATOM 1970 NH1 ARG 301 35.040 38.534 46.343 1.00 13.79 1DLC2094 ATOM 1971 NH2 ARG 301 35.667 39.613 44.420 1.00 14.12 1DLC2095 ATOM 1972 N ASP 302 31.690 38.370 49.478 1.00 19.99 1DLC2096 ATOM 1973 CA ASP 302 31.196 37.161 48.817 1.00 20.22 1DLC2097 ATOM 1974 C ASP 302 30.662 37.483 47.432 1.00 20.75 1DLC2098 ATOM 1975 O ASP 302 30.141 38.573 47.196 1.00 24.04 1DLC2099 ATOM 1976 CB ASP 302 29.980 36.582 49.556 1.00 24.46 1DLC2100 ATOM 1977 CG ASP 302 30.316 35.978 50.886 1.00 31.05 1DLC2101 ATOM 1978 OD1 ASP 302 31.510 35.740 51.162 1.00 41.38 1DLC2102 ATOM 1979 OD2 ASP 302 29.363 35.721 51.657 1.00 34.73 1DLC2103 ATOM 1980 N VAL 303 30.741 36.501 46.544 1.00 18.31 1DLC2104 ATOM 1981 CA VAL 303 30.182 36.601 45.199 1.00 18.50 1DLC2105 ATOM 1982 C VAL 303 29.592 35.219 44.926 1.00 17.19 1DLC2106 ATOM 1983 O VAL 303 30.131 34.204 45.370 1.00 18.03 1DLC2107 ATOM 1984 CB VAL 303 31.204 37.008 44.094 1.00 19.37 1DLC2108 ATOM 1985 CG1 VAL 303 31.744 38.402 44.369 1.00 21.25 1DLC2109 ATOM 1986 CG2 VAL 303 32.328 35.992 43.973 1.00 21.50 1DLC2110 ATOM 1987 N LEU 304 28.410 35.201 44.330 1.00 16.94 1DLC2111 ATOM 1988 CA LEU 304 27.713 33.962 44.022 1.00 13.97 1DLC2112 ATOM 1989 C LEU 304 27.764 33.726 42.527 1.00 14.14 1DLC2113 ATOM 1990 O LEU 304 27.474 34.622 41.730 1.00 13.74 1DLC2114 ATOM 1991 CB LEU 304 26.235 34.053 44.433 1.00 14.18 1DLC2115 ATOM 1992 CG LEU 304 25.680 34.294 45.846 1.00 13.89 1DLC2116 ATOM 1993 CD1 LEU 304 25.252 32.993 46.457 1.00 14.90 1DLC2117 ATOM 1994 CD2 LEU 304 26.641 35.052 46.745 1.00 11.27 1DLC2118 ATOM 1995 N THR 305 28.146 32.521 42.140 1.00 14.38 1DLC2119 ATOM 1996 CA THR 305 28.175 32.187 40.721 1.00 16.18 1DLC2120 ATOM 1997 C THR 305 26.737 31.864 40.282 1.00 17.39 1DLC2121 ATOM 1998 O THR 305 25.845 31.688 41.124 1.00 15.94 1DLC2122 ATOM 1999 CB THR 305 29.115 30.969 40.422 1.00 17.34 1DLC2123 ATOM 2000 OG1 THR 305 29.021 30.000 41.475 1.00 19.98 1DLC2124 ATOM 2001 CG2 THR 305 30.565 31.415 40.270 1.00 18.26 1DLC2125 ATOM 2002 N ASP 306 26.488 31.891 38.978 1.00 15.04 1DLC2126 ATOM 2003 CA ASP 306 25.177 31.551 38.437 1.00 17.79 1DLC2127 ATOM 2004 C ASP 306 24.785 30.157 38.913 1.00 21.19 1DLC2128 ATOM 2005 O ASP 306 25.651 29.278 39.067 1.00 24.55 1DLC2129 ATOM 2006 CB ASP 306 25.222 31.530 36.912 1.00 15.07 1DLC2130 ATOM 2007 CG ASP 306 25.286 32.905 36.310 1.00 15.88 1DLC2131 ATOM 2008 OD1 ASP 306 24.822 33.867 36.946 1.00 18.05 1DLC2132 ATOM 2009 OD2 ASP 306 25.777 33.024 35.174 1.00 23.36 1DLC2133 ATOM 2010 N PRO 307 23.483 29.938 39.179 1.00 22.83 1DLC2134 ATOM 2011 CA PRO 307 23.004 28.623 39.639 1.00 20.21 1DLC2135 ATOM 2012 C PRO 307 23.289 27.551 38.587 1.00 16.74 1DLC2136 ATOM 2013 O PRO 307 23.289 27.827 37.389 1.00 17.78 1DLC2137 ATOM 2014 CB PRO 307 21.502 28.848 39.811 1.00 20.31 1DLC2138 ATOM 2015 CG PRO 307 21.410 30.306 40.150 1.00 21.80 1DLC2139 ATOM 2016 CD PRO 307 22.388 30.925 39.175 1.00 20.89 1DLC2140 ATOM 2017 N ILE 308 23.547 26.333 39.033 1.00 18.04 1DLC2141 ATOM 2018 CA ILE 308 23.851 25.245 38.107 1.00 19.10 1DLC2142 ATOM 2019 C ILE 308 22.579 24.514 37.684 1.00 21.11 1DLC2143 ATOM 2020 O ILE 308 22.004 23.759 38.473 1.00 23.40 1DLC2144 ATOM 2021 CB ILE 308 24.833 24.227 38.753 1.00 20.63 1DLC2145 ATOM 2022 CG1 ILE 308 25.992 24.971 39.439 1.00 21.46 1DLC2146 ATOM 2023 CG2 ILE 308 25.352 23.252 37.700 1.00 19.02 1DLC2147 ATOM 2024 CD1 ILE 308 26.923 24.082 40.247 1.00 17.99 1DLC2148 ATOM 2025 N VAL 309 22.119 24.763 36.460 1.00 23.15 1DLC2149 ATOM 2026 CA VAL 309 20.907 24.108 35.944 1.00 25.59 1DLC2150 ATOM 2027 C VAL 309 21.139 23.415 34.602 1.00 25.03 1DLC2151 ATOM 2028 O VAL 309 21.908 23.891 33.778 1.00 24.20 1DLC2152 ATOM 2029 CB VAL 309 19.689 25.093 35.800 1.00 23.31 1DLC2153 ATOM 2030 CG1 VAL 309 19.295 25.652 37.160 1.00 24.72 1DLC2154 ATOM 2031 CG2 VAL 309 20.005 26.214 34.847 1.00 25.99 1DLC2155 ATOM 2032 N GLY 310 20.462 22.290 34.393 1.00 26.11 1DLC2156 ATOM 2033 CA GLY 310 20.610 21.549 33.151 1.00 28.39 1DLC2157 ATOM 2034 C GLY 310 19.889 22.100 31.926 1.00 31.24 1DLC2158 ATOM 2035 O GLY 310 20.257 21.777 30.802 1.00 35.55 1DLC2159 ATOM 2036 N GLY 310 18.866 22.927 32.128 1.00 32.38 1DLC2160 ATOM 2037 CA VAL 311 18.102 23.498 31.012 1.00 30.87 1DLC2161 ATOM 2038 C VAL 311 18.111 25.024 31.105 1.00 29.77 1DLC2162 ATOM 2039 O VAL 311 18.175 25.648 32.070 1.00 31.01 1DLC2163 ATOM 2040 CB VAL 311 16.616 23.022 31.028 1.00 31.20 1DLC2164 ATOM 2041 CG1 VAL 311 16.525 21.524 30.803 1.00 32.24 1DLC2165 ATOM 2042 CG2 VAL 311 15.966 23.374 32.347 1.00 28.27 1DLC2166 ATOM 2043 N ASN 312 17.976 25.613 29.832 1.00 34.45 1DLC2167 ATOM 2044 CA ASN 312 17.968 27.071 29.683 1.00 38.67 1DLC2168 ATOM 2045 C ASN 312 16.678 27.741 30.145 1.00 37.69 1DLC2169 ATOM 2046 O ASN 312 16.696 28.874 30.619 1.00 39.59 1DLC2170 ATOM 2047 CB ASN 312 18.219 27.462 28.225 1.00 46.17 1DLC2171 ATOM 2048 CG ASN 312 19.670 27.287 27.806 1.00 53.31 1DLC2172 ATOM 2049 OD1 ASN 312 20.581 27.275 28.638 1.00 56.28 1DLC2173 ATOM 2050 ND2 ASN 312 19.894 27.181 26.500 1.00 59.74 1DLC2174 ATOM 2051 N ASN 313 15.559 27.048 29.963 1.00 35.04 1DLC2175 ATOM 2052 CA ASN 313 14.243 27.559 30.339 1.00 31.97 1DLC2176 ATOM 2053 C ASN 313 13.538 26.549 31.247 1.00 30.91 1DLC2177 ATOM 2054 O ASN 313 13.221 25.432 30.819 1.00 32.94 1DLC2178 ATOM 2055 CB ASN 313 13.427 27.807 29.065 1.00 31.98 1DLC2179 ATOM 2056 CG ASN 313 12.051 28.364 29.339 1.00 29.11 1DLC2180 ATOM 2057 OD1 ASN 313 11.646 28.542 30.486 1.00 31.35 1DLC2181 ATOM 2058 ND2 ASN 313 11.322 28.651 28.279 1.00 26.80 1DLC2182 ATOM 2059 N LEU 314 13.295 26.950 32.493 1.00 26.72 1DLC2183 ATOM 2060 CA LEU 314 12.648 26.991 33.486 1.00 24.82 1DLC2184 ATOM 2061 C LEU 314 11.114 26.096 33.478 1.00 26.88 1DLC2185 ATOM 2062 O LEU 314 10.483 25.503 34.363 1.00 29.59 1DLC2186 ATOM 2063 CB LEU 314 13.151 26.432 34.891 1.00 21.60 1DLC2187 ATOM 2064 CG LEU 314 14.519 25.889 35.295 1.00 22.09 1DLC2188 ATOM 2065 CD1 LEU 314 14.849 26.325 36.707 1.00 20.63 1DLC2189 ATOM 2066 CD2 LEU 314 14.510 24.373 35.217 1.00 20.55 1DLC2190 ATOM 2067 N ARG 315 10.525 26.768 32.491 1.00 24.99 1DLC2191 ATOM 2068 CA ARG 315 9.072 26.865 32.353 1.00 24.53 1DLC2192 ATOM 2069 C ARG 315 8.306 27.125 33.659 1.00 21.66 1DLC2193 ATOM 2070 O ARG 315 7.305 26.478 33.947 1.00 25.12 1DLC2194 ATOM 2071 CB ARG 315 8.508 25.640 31.619 1.00 28.28 1DLC2195 ATOM 2072 CG ARG 315 8.737 25.652 30.105 1.00 34.47 1DLC2196 ATOM 2073 CD ARG 315 7.977 24.524 29.387 1.00 45.54 1DLC2197 ATOM 2074 NE ARG 315 6.513 24.685 29.412 1.00 59.49 1DLC2198 ATOM 2075 CZ ARG 315 5.682 24.048 30.246 1.00 63.23 1DLC2199 ATOM 2076 NH1 ARG 315 6.149 23.191 31.149 1.00 65.85 1DLC2200 ATOM 2077 NH2 ARG 315 4.373 24.264 30.179 1.00 62.27 1DLC2201 ATOM 2078 N GLY 316 8.807 28.060 34.458 1.00 21.30 1DLC2202 ATOM 2079 CA GLY 316 8.151 28.420 35.704 1.00 16.98 1DLC2203 ATOM 2080 C GLY 316 8.497 27.638 36.953 1.00 18.35 1DLC2204 ATOM 2081 O GLY 316 8.082 28.010 38.049 1.00 17.47 1DLC2205 ATOM 2082 N TYR 317 9.256 26.561 36.812 1.00 20.77 1DLC2206 ATOM 2083 CA TYR 317 9.615 25.751 37.971 1.00 20.18 1DLC2207 ATOM 2084 C TYR 317 10.806 26.243 38.782 1.00 21.76 1DLC2208 ATOM 2085 O TYR 317 11.103 25.704 39.847 1.00 24.15 1DLC2209 ATOM 2086 CB TYR 317 9.800 24.298 37.554 1.00 22.63 1DLC2210 ATOM 2087 CG TYR 317 8.497 23.648 37.192 1.00 23.66 1DLC2211 ATOM 2088 CD1 TYR 317 7.703 23.062 38.171 1.00 25.39 1DLC2212 ATOM 2089 CD2 TYR 317 8.027 23.668 35.882 1.00 24.11 1DLC2213 ATOM 2090 CE1 TYR 317 6.469 22.512 37.860 1.00 27.42 1DLC2214 ATOM 2091 CE2 TYR 317 6.795 23.127 35.557 1.00 27.40 1DLC2215 ATOM 2092 CZ TYR 317 6.018 22.551 36.557 1.00 29.75 1DLC2216 ATOM 2093 OH TYR 317 4.782 22.026 36.262 1.00 34.32 1DLC2217 ATOM 2094 N GLY 318 11.475 27.281 38.300 1.00 20.77 1DLC2218 ATOM 2095 CA GLY 318 12.608 27.810 39.029 1.00 18.55 1DLC2219 ATOM 2096 C GLY 318 12.210 28.393 40.374 1.00 19.44 1DLC2220 ATOM 2097 O GLY 318 11.130 28.977 40.519 1.00 20.54 1DLC2221 ATOM 2098 N THR 319 13.069 28.209 41.369 1.00 17.62 1DLC2222 ATOM 2099 CA THR 319 12.834 28.739 42.712 1.00 17.45 1DLC2223 ATOM 2100 C THR 319 12.556 30.236 42.630 1.00 20.62 1DLC2224 ATOM 2101 O THR 319 13.184 30.941 41.842 1.00 25.06 1DLC2225 ATOM 2102 CB THR 319 14.075 28.548 43.573 1.00 17.42 1DLC2226 ATOM 2103 OG1 THR 319 14.492 27.180 43.496 1.00 21.15 1DLC2227 ATOM 2104 CG2 THR 319 13.794 28.924 45.012 1.00 14.83 1DLC2228 ATOM 2105 N THR 320 11.631 30.732 43.440 1.00 19.91 1DLC2229 ATOM 2106 CA THR 320 11.307 32.157 43.398 1.00 18.68 1DLC2230 ATOM 2107 C THR 320 12.414 33.064 43.936 1.00 20.02 1DLC2231 ATOM 2108 O THR 320 13.210 32.666 44.790 1.00 24.12 1DLC2232 ATOM 2109 CB THR 320 9.997 32.468 44.141 1.00 16.01 1DLC2233 ATOM 2110 OG1 THR 320 10.095 32.022 45.493 1.00 19.03 1DLC2234 ATOM 2111 CG2 THR 320 8.848 31.775 43.477 1.00 10.83 1DLC2235 ATOM 2112 N PHE 321 12.446 34.291 43.431 1.00 18.76 1DLC2236 ATOM 2113 CA PHE 321 13.430 35.292 43.835 1.00 18.42 1DLC2237 ATOM 2114 C PHE 321 13.600 35.328 45.359 1.00 19.97 1DLC2238 ATOM 2115 O PHE 321 14.700 35.142 45.882 1.00 18.92 1DLC2239 ATOM 2116 CB PHE 321 12.990 36.666 43.311 1.00 18.89 1DLC2240 ATOM 2117 CG PHE 321 14.009 37.758 43.500 1.00 20.25 1DLC2241 ATOM 2118 CD1 PHE 321 14.366 38.199 44.776 1.00 19.19 1DLC2242 ATOM 2119 CD2 PHE 321 14.589 38.373 42.398 1.00 18.51 1DLC2243 ATOM 2120 CE1 PHE 321 15.279 39.235 44.947 1.00 20.39 1DLC2244 ATOM 2121 qE2 PHE 321 15.504 39.412 42.560 1.00 19.17 1DLC2245 ATOM 2122 CZ PHE 321 15.849 39.844 43.835 1.00 21.01 1DLC2246 ATOM 2123 N SER 322 12.497 35.528 46.069 1.00 21.66 1DLC2247 ATOM 2124 CA SER 322 12.527 35.587 47.531 1.00 23.88 1DLC2248 ATOM 2125 C SER 322 12.978 34.310 48.220 1.00 21.84 1DLC2249 ATOM 2126 O SER 322 13.594 34.361 49.283 1.00 23.06 1DLC2250 ATOM 2127 CB SER 322 11.176 36.030 48.079 1.00 24.50 1DLC2251 ATOM 2128 OG SER 322 10.894 37.344 47.621 1.00 37.62 1DLC2252 ATOM 2129 N ASN 323 12.695 33.163 47.614 1.00 22.20 1DLC2253 ATOM 2130 CA ASN 323 13.117 31.900 48.208 1.00 23.04 1DLC2254 ATOM 2131 C ASN 323 14.606 31.623 48.007 1.00 21.38 1DLC2255 ATOM 2132 O ASN 323 15.159 30.688 48.582 1.00 22.81 1DLC2256 ATOM 2133 CB ASN 323 12.250 30.743 47.732 1.00 24.92 1DLC2257 ATOM 2134 CG ASN 323 10.897 30.730 48.408 1.00 25.16 1DLC2258 ATOM 2135 OD1 ASN 323 10.741 31.216 49.525 1.00 26.34 1DLC2259 ATOM 2136 ND2 ASN 323 9.909 30.193 47.727 1.00 29.75 1DLC2260 ATOM 2137 N ILE 324 15.240 32.426 47.160 1.00 19.13 1DLC2261 ATOM 2138 CA ILE 324 16.672 32.318 46.961 1.00 17.26 1DLC2262 ATOM 2139 C ILE 324 17.340 33.454 47.759 1.00 18.23 1DLC2263 ATOM 2140 O ILE 324 18.050 33.214 48.742 1.00 18.12 1DLC2264 ATOM 2141 CB ILE 324 17.073 32.449 45.485 1.00 13.05 1DLC2265 ATOM 2142 CG1 ILE 324 16.380 31.379 44.655 1.00 10.69 1DLC2266 ATOM 2143 CG2 ILE 324 18.584 32.294 45.342 1.00 13.12 1DLC2267 ATOM 2144 CD1 ILE 324 16.771 31.402 43.202 1.00 11.56 1DLC2268 ATOM 2145 N GLU 325 17.014 34.693 47.399 1.00 17.70 1DLC2269 ATOM 2146 CA GLU 325 17.608 35.866 48.038 1.00 19.04 1DLC2270 ATOM 2147 C GLU 325 17.473 35.948 49.560 1.00 21.70 1DLC2271 ATOM 2148 O GLU 325 18.416 36.347 50.242 1.00 23.28 1DLC2272 ATOM 2149 CB GLU 325 17.117 37.149 47.356 1.00 20.14 1DLC2273 ATOM 2150 CG GLU 325 17.856 38.439 47.749 1.00 19.56 1DLC2274 ATOM 2151 CD GLU 325 19.369 38.422 47.477 1.00 19.74 1DLC2275 ATOM 2152 OE1 GLU 325 19.836 37.805 46.497 1.00 19.17 1DLC2276 ATOM 2153 OE2 GLU 325 20.104 39.056 48.259 1.00 21.56 1DLC2277 ATOM 2154 N ASN 326 16.333 35.529 50.100 1.00 22.82 1DLC2278 ATOM 2155 CA ASN 326 16.133 35.568 51.546 1.00 21.61 1DLC2279 ATOM 2156 C ASN 326 16.849 34.441 52.271 1.00 22.46 1DLC2280 ATOM 2157 O ASN 326 16.948 34.449 53.499 1.00 22.03 1DLC2281 ATOM 2158 CB ASN 326 14.646 35.512 51.891 1.00 25.83 1DLC2282 ATOM 2159 CG ASN 326 13.912 36.795 51.551 1.00 30.73 1DLC2283 ATOM 2160 OD1 ASN 326 12.713 36.784 51.298 1.00 36.78 1DLC2284 ATOM 2161 ND2 ASN 326 14.621 37.907 51.556 1.00 33.22 1DLC2285 ATOM 2162 N TYR 327 17.346 33.469 51.515 1.00 21.89 1DLC2286 ATOM 2163 CA TYR 327 18.023 32.335 52.128 1.00 23.83 1DLC2287 ATOM 2164 C TYR 327 19.516 32.203 51.912 1.00 22.96 1DLC2288 ATOM 2165 O TYR 327 20.148 31.355 52.533 1.00 27.36 1DLC2289 ATOM 2166 CB TYR 327 17.313 31.034 51.773 1.00 30.00 1DLC2290 ATOM 2167 CG TYR 327 15.943 30.955 52.399 1.00 33.84 1DLC2291 ATOM 2168 CD1 TYR 327 14.835 31.495 51.755 1.00 32.53 1DLC2292 ATOM 2169 CD2 TYR 327 15.761 30.363 53.648 1.00 34.52 1DLC2293 ATOM 2170 CE1 TYR 327 13.589 31.452 52.333 1.00 36.59 1DLC2294 ATOM 2171 CE2 TYR 327 14.511 30.313 54.239 1.00 36.84 1DLC2295 ATOM 2172 CZ TYR 327 13.427 30.859 53.574 1.00 39.48 1DLC2296 ATOM 2173 OH TYR 327 12.167 30.805 54.138 1.00 48.47 1DLC2297 ATOM 2174 N ILE 328 20.085 33.005 51.020 1.00 20.63 1DLC2298 ATOM 2175 CA ILE 328 21.525 32.955 50.813 1.00 19.45 1DLC2299 ATOM 2176 C ILE 328 22.176 33.473 52.102 1.00 23.48 1DLC2300 ATOM 2177 O ILE 328 21.511 34.124 52.919 1.00 24.83 1DLC2301 ATOM 2178 CB ILE 328 21.977 33.815 49.610 1.00 17.68 1DLC2302 ATOM 2179 CG1 ILE 328 21.666 35.292 49.842 1.00 19.52 1DLC2303 ATOM 2180 CG2 ILE 328 21.308 33.332 48.348 1.00 15.95 1DLC2304 ATOM 2181 CD1 ILE 328 22.220 36.207 48.778 1.00 18.88 1DLC2305 ATOM 2182 N ARG 329 23.457 33.161 52.296 1.00 24.81 1DLC2306 ATOM 2183 CA ARG 329 24.207 33.576 53.486 1.00 21.84 1DLC2307 ATOM 2184 C ARG 329 24.091 35.065 53.820 1.00 22.27 1DLC2308 ATOM 2185 O ARG 329 24.268 35.917 52.953 1.00 25.04 1DLC2309 ATOM 2186 CB ARG 329 25.683 33.242 53.299 1.00 23.15 1DLC2310 ATOM 2187 CG ARG 329 25.990 31.776 53.243 1.00 24.82 1DLC2311 ATOM 2188 CD ARG 329 26.732 31.373 54.501 1.00 28.71 1DLC2312 ATOM 2189 NE ARG 329 28.173 31.390 54.297 1.00 24.15 1DLC2313 ATOM 2190 CZ ARG 329 29.077 31.204 55.256 1.00 23.69 1DLC2314 ATOM 2191 NH1 ARG 329 28.710 30.996 56.515 1.00 13.74 1DLC2315 ATOM 2192 NH2 ARG 329 30.360 31.179 54.937 1.00 20.55 1DLC2316 ATOM 2193 N LYS 330 23.804 35.373 55.080 1.00 24.03 1DLC2317 ATOM 2194 CA LYS 330 23.696 36.763 55.533 1.00 24.69 1DLC2318 ATOM 2195 C LYS 330 25.041 37.243 56.085 1.00 22.84 1DLC2319 ATOM 2196 O LYS 330 25.929 36.428 56.345 1.00 22.64 1DLC2320 ATOM 2197 CB LYS 330 22.608 36.896 56.605 1.00 27.12 1DLC2321 ATOM 2198 CG LYS 330 21.199 36.885 56.033 1.00 33.76 1DLC2322 ATOM 2199 CD LYS 330 20.164 37.200 57.096 1.00 42.42 1DLC2323 ATOM 2200 CE LYS 330 18.753 37.179 56.510 1.00 47.90 1DLC2324 ATOM 2201 NZ LYS 330 18.405 35.828 55.959 1.00 53.46 1DLC2325 ATOM 2202 N PRO 331 25.219 38.568 56.245 1.00 22.24 1DLC2326 ATOM 2203 CA PRO 331 26.479 39.105 56.771 1.00 20.54 1DLC2327 ATOM 2204 C PRO 331 27.000 38.248 57.913 1.00 21.52 1DLC2328 ATOM 2205 O PRO 331 26.327 38.053 58.918 1.00 23.22 1DLC2329 ATOM 2206 CB PRO 331 26.079 40.497 57.230 1.00 21.52 1DLC2330 ATOM 2207 CG PRO 331 25.100 40.898 56.163 1.00 19.00 1DLC2331 ATOM 2208 CD PRO 331 24.252 39.654 55.996 1.00 19.95 1DLC2332 ATOM 2209 N HIS 332 28.193 37.700 57.715 1.00 21.33 1DLC2333 ATOM 2210 CA HIS 332 28.810 36.810 58.682 1.00 18.59 1DLC2334 ATOM 2211 C HIS 332 30.310 37.019 58.847 1.00 19.87 1DLC2335 ATOM 2212 O HIS 332 30.991 37.511 57.949 1.00 19.56 1DLC2336 ATOM 2213 CB HIS 332 28.597 35.371 58.214 1.00 14.92 1DLC2337 ATOM 2214 CG HIS 332 29.196 35.084 56.870 1.00 13.36 1DLC2338 ATOM 2215 ND1 HIS 332 30.474 34.589 56.712 1.00 17.22 1DLC2339 ATOM 2216 CD2 HIS 332 28.700 35.242 55.619 1.00 13.52 1DLC2340 ATOM 2217 CE1 HIS 332 30.741 34.454 55.425 1.00 16.38 1DLC2341 ATOM 2218 NE2 HIS 332 29.680 34.843 54.740 1.00 18.37 1DLC2342 ATOM 2219 N LEU 333 30.828 36.585 59.987 1.00 20.07 1DLC2343 ATOM 2220 CA LEU 333 32.260 36.643 60.259 1.00 17.84 1DLC2344 ATOM 2221 C LEU 333 32.883 35.741 59.180 1.00 18.07 1DLC2345 ATOM 2222 O LEU 333 32.246 34.784 58.719 1.00 19.71 1DLC2346 ATOM 2223 CB LEU 333 32.518 36.070 61.651 1.00 12.65 1DLC2347 ATOM 2224 CG LEU 333 33.158 36.944 62.721 1.00 14.26 1DLC2348 ATOM 2225 CD1 LEU 333 32.855 38.403 62.506 1.00 13.22 1DLC2349 ATOM 2226 CD2 LEU 333 32.689 36.472 64.083 1.00 9.06 1DLC2350 ATOM 2227 N PHE 334 34.089 36.065 58.738 1.00 16.81 1DLC2351 ATOM 2228 CA PHE 334 34.756 35.294 57.689 1.00 16.45 1DLC2352 ATOM 2229 C PHE 334 35.055 33.841 58.074 1.00 18.71 1DLC2353 ATOM 2230 O PHE 334 35.438 33.562 59.217 1.00 21.26 1DLC2354 ATOM 2231 CB PHE 334 36.053 35.994 57.257 1.00 16.25 1DLC2355 ATOM 2232 CG PHE 334 36.519 35.602 55.891 1.00 15.09 1DLC2356 ATOM 2233 CD1 PHE 334 37.286 34.455 55.702 1.00 13.90 1DLC2357 ATOM 2234 CD2 PHE 334 36.141 36.350 54.779 1.00 13.34 1DLC2358 ATOM 2235 CE1 PHE 334 37.663 34.056 54.422 1.00 11.52 1DLC2359 ATOM 2236 CE2 PHE 334 36.516 35.958 53.496 1.00 14.32 1DLC2360 ATOM 2237 CZ PHE 334 37.278 34.806 53.318 1.00 12.48 1DLC2361 ATOM 2238 N ASP 335 34.851 32.919 57.133 1.00 14.83 1DLC2362 ATOM 2239 CA ASP 335 35.125 31.501 57.382 1.00 15.09 1DLC2363 ATOM 2240 C ASP 335 35.576 30.773 56.119 1.00 15.60 1DLC2364 ATOM 2241 D ASP 335 35.592 31.359 55.040 1.00 17.59 1DLC2365 ATOM 2242 CB ASP 335 33.941 30.783 58.058 1.00 15.88 1DLC2366 ATOM 2243 CG ASP 335 32.678 30.752 57.198 1.00 17.94 1DLC2367 ATOM 2244 OD1 ASP 335 32.750 30.903 55.958 1.00 17.49 1DLC2368 ATOM 2245 OD2 ASP 335 31.595 30.553 57.780 1.00 20.32 1DLC2369 ATOM 2246 N TYR 336 35.922 29.498 56.248 1.00 15.68 1DLC2370 ATOM 2247 CA TYR 336 36.415 28.728 55.109 1.00 17.74 1DLC2371 ATOM 2248 C TYR 336 35.711 27.387 54.888 1.00 17.85 1DLC2372 ATOM 2249 D TYR 336 35.266 26.734 55.836 1.00 17.36 1DLC2373 ATOM 2250 CB TYR 336 37.918 28.494 55.284 1.00 18.22 1DLC2374 ATOM 2251 CG TYR 336 38.700 29.753 55.593 1.00 21.42 1DLC2375 ATOM 2252 CD1 TYR 336 38.688 30.310 56.874 1.00 20.91 1DLC2376 ATOM 2253 CD2 TYR 336 39.437 30.398 54.597 1.00 23.29 1DLC2377 ATOM 2254 CE1 TYR 336 39.389 31.481 57.153 1.00 25.49 1DLC2378 ATOM 2255 CE2 TYR 336 40.147 31.567 54.865 1.00 24.79 1DLC2379 ATOM 2256 CZ TYR 336 40.119 32.105 56.142 1.00 25.10 1DLC2380 ATOM 2257 OH TYR 336 40.820 33.262 56.402 1.00 25.35 1DLC2381 ATOM 2258 N LEU 337 35.634 26.968 53.631 1.00 17.01 1DLC2382 ATOM 2259 CA LEU 337 34.999 25.701 53.284 1.00 22.05 1DLC2383 ATOM 2260 C LEU 337 35.753 24.564 53.983 1.00 25.09 1DLC2384 ATOM 2261 O LEU 337 36.971 24.429 53.851 1.00 27.06 1DLC2385 ATOM 2262 CB LEU 337 35.041 25.493 51.765 1.00 19.73 1DLC2386 ATOM 2263 CG LEU 337 34.001 24.618 51.045 1.00 20.25 1DLC2387 ATOM 2264 CD1 LEU 337 34.715 23.668 50.117 1.00 16.93 1DLC2388 ATOM 2265 CD2 LEU 337 33.109 23.867 52.007 1.00 15.63 1DLC2389 ATOM 2266 N HIS 338 35.038 23.753 54.746 1.00 27.56 1DLC2390 ATOM 2267 CA HIS 338 35.686 22.654 55.447 1.00 32.45 1DLC2391 ATOM 2268 C HIS 338 35.223 21.263 55.002 1.00 35.81 1DLC2392 ATOM 2269 O HIS 338 36.040 20.350 54.825 1.00 37.52 1DLC2393 ATOM 2270 CB HIS 338 35.485 22.810 56.952 1.00 31.95 1DLC2394 ATOM 2271 CG HIS 338 36.423 21.983 57.771 1.00 35.39 1DLC2395 ATOM 2272 ND1 HIS 338 36.028 20.835 58.424 1.00 39.61 1DLC2396 ATOM 2273 CD2 HIS 338 37.740 22.140 58.047 1.00 35.97 1DLC2397 ATOM 2274 CE1 HIS 338 37.060 20.320 59.070 1.00 39.82 1DLC2398 ATOM 2275 NE2 HIS 338 38.110 21.093 58.856 1.00 39.08 1DLC2399 ATOM 2276 N ARG 339 33.918 21.111 54.801 1.00 36.63 1DLC2400 ATOM 2277 CA ARG 339 33.361 19.824 54.417 1.00 37.71 1DLC2401 ATOM 2278 C ARG 339 32.016 19.948 53.704 1.00 35.21 1DLC2402 ATOM 2279 O ARG 339 31.294 20.928 53.889 1.00 34.83 1DLC2403 ATOM 2280 CB ARG 339 33.231 18.972 55.684 1.00 43.00 1DLC2404 ATOM 2281 CG ARG 339 32.608 17.602 55.526 1.00 48.56 1DLC2405 ATOM 2282 CD ARG 339 33.140 16.657 56.611 1.00 57.10 1DLC2406 ATOM 2283 NE ARG 339 33.391 17.338 57.888 1.00 62.49 1DLC2407 ATOM 2284 CZ ARG 339 34.520 17.235 58.597 1.00 63.78 1DLC2408 ATOM 2285 NH1 ARG 339 35.521 16.474 58.171 1.00 61.26 1DLC2409 ATOM 2286 NH2 ARG 339 34.651 17.905 59.739 1.00 63.23 1DLC2410 ATOM 2287 N ILE 340 31.717 18.981 52.842 1.00 33.04 1DLC2411 ATOM 2288 CA ILE 340 30.449 18.957 52.113 1.00 31.15 1DLC2412 ATOM 2289 C ILE 340 29.828 17.554 52.094 1.00 31.37 1DLC2413 ATOM 2290 O ILE 340 30.512 16.560 51.809 1.00 32.64 1DLC2414 ATOM 2291 CB ILE 340 30.594 19.440 50.642 1.00 28.39 1DLC2415 ATOM 2292 CG1 ILE 340 31.263 20.812 50.588 1.00 26.45 1DLC2416 ATOM 2293 CG2 ILE 340 29.204 19.547 49.988 1.00 23.66 1DLC2417 ATOM 2294 CD1 ILE 340 31.491 21.316 49.181 1.00 23.48 1DLC2418 ATOM 2295 N GLN 341 28.542 17.475 52.430 1.00 29.86 1DLC2419 ATOM 2296 CA GLN 341 27.831 16.202 52.415 1.00 28.77 1DLC2420 ATOM 2297 C GLN 341 26.799 16.150 51.292 1.00 27.88 1DLC2421 ATOM 2298 O GLN 341 25.717 16.733 51.391 1.00 29.80 1DLC2422 ATOM 2299 CB GLN 341 27.153 15.903 53.752 1.00 27.96 1DLC2423 ATOM 2300 CG GLN 341 26.387 14.584 53.704 1.00 34.48 1DLC2424 ATOM 2301 CD GLN 341 25.905 14.100 55.057 1.00 37.10 1DLC2425 ATOM 2302 OE1 GLN 341 24.703 13.989 55.297 1.00 39.41 1DLC2426 ATOM 2303 NE2 GLN 341 26.834 13.776 55.932 1.00 37.68 1DLC2427 ATOM 2304 N PHE 342 27.143 15.439 50.228 1.00 27.45 1DLC2428 ATOM 2305 CA PHE 342 26.264 15.287 49.076 1.00 28.97 1DLC2429 ATOM 2306 C PHE 342 25.153 14.251 49.253 1.00 29.10 1DLC2430 ATOM 2307 O PHE 342 25.377 13.152 49.760 1.00 30.40 1DLC2431 ATOM 2308 CB PHE 342 27.081 14.942 47.831 1.00 27.31 1DLC2432 ATOM 2309 CG PHE 342 27.994 16.038 47.389 1.00 26.99 1DLC2433 ATOM 2310 CD1 PHE 342 29.200 16.257 48.036 1.00 28.62 1DLC2434 ATOM 2311 CD2 PHE 342 27.646 16.860 46.327 1.00 27.99 1DLC2435 ATOM 2312 CE1 PHE 342 30.045 17.281 47.631 1.00 29.72 1DLC2436 ATOM 2313 CE2 PHE 342 28.484 17.886 45.915 1.00 28.28 1DLC2437 ATOM 2314 CZ PHE 342 29.684 18.096 46.568 1.00 29.89 1DLC2438 ATOM 2315 N HIS 343 23.936 14.647 48.898 1.00 31.24 1DLC2439 ATOM 2316 CA HIS 343 22.780 13.760 48.966 1.00 30.73 1DLC2440 ATOM 2317 C HIS 343 22.330 13.517 47.544 1.00 30.25 1DLC2441 ATOM 2318 O HIS 343 22.214 14.456 46.760 1.00 30.83 1DLC2442 ATOM 2319 CB HIS 343 21.644 14.367 49.786 1.00 27.80 1DLC2443 ATOM 2320 CG HIS 343 21.840 14.231 51.263 1.00 28.77 1DLC2444 ATOM 2321 ND1 HIS 343 22.925 14.766 51.922 1.00 32.44 1DLC2445 ATOM 2322 CD2 HIS 343 21.101 13.601 52.207 1.00 27.79 1DLC2446 ATOM 2323 CE1 HIS 343 22.849 14.472 53.205 1.00 30.66 1DLC2447 ATOM 2324 NE2 HIS 343 21.751 13.766 53.404 1.00 30.61 1DLC2448 ATOM 2325 N THR 344 22.118 12.248 47.214 1.00 30.51 1DLC2449 ATOM 2326 CA THR 344 21.707 11.853 45.873 1.00 30.88 1DLC2450 ATOM 2327 C THR 344 20.344 11.154 45.812 1.00 33.44 1DLC2451 ATOM 2328 O THR 344 19.928 10.442 46.744 1.00 32.56 1DLC2452 ATOM 2329 CB THR 344 22.775 10.938 45.225 1.00 26.81 1DLC2453 ATOM 2330 OG1 THR 344 24.046 11.597 45.262 1.00 29.11 1DLC2454 ATOM 2331 CG2 THR 344 22.430 10.614 43.785 1.00 24.42 1DLC2455 ATOM 2332 N ARG 345 19.655 11.385 44.698 1.00 32.36 1DLC2456 ATOM 2333 CA ARG 345 18.352 10.796 44.433 1.00 29.58 1DLC2457 ATOM 2334 C ARG 345 18.289 10.272 43.010 1.00 29.62 1DLC2458 ATOM 2335 O ARG 345 19.079 10.681 42.145 1.00 27.21 1DLC2459 ATOM 2336 CB ARG 345 17.233 11.812 44.659 1.00 26.82 1DLC2460 ATOM 2337 CG ARG 345 16.905 12.019 46.118 1.00 25.81 1DLC2461 ATOM 2338 CD ARG 345 15.509 12.552 46.288 1.00 25.24 1DLC2462 ATOM 2339 NE ARG 345 15.127 12.531 47.692 1.00 30.00 1DLC2463 ATOM 2340 CZ ARG 345 13.978 12.998 48.167 1.00 32.09 1DLC2464 ATOM 2341 NH1 ARG 345 13.076 13.525 47.348 1.00 32.16 1DLC2465 ATOM 2342 NH2 ARG 345 13.749 12.978 49.473 1.00 33.30 1DLC2466 ATOM 2343 N PHE 346 17.391 9.316 42.796 1.00 27.16 1DLC2467 ATOM 2344 CA PHE 346 17.193 8.715 41.487 1.00 26.42 1DLC2468 ATOM 2345 C PHE 346 16.082 9.404 40.701 1.00 26.65 1DLC2469 ATOM 2346 O PHE 346 15.003 9.651 41.224 1.00 27.28 1DLC2470 ATOM 2347 CB PHE 346 16.875 7.222 41.633 1.00 25.70 1DLC2471 ATOM 2348 CG PHE 346 16.431 6.565 40.349 1.00 24.42 1DLC2472 ATOM 2349 CD1 PHE 346 17.296 6.461 39.267 1.00 25.47 1DLC2473 ATOM 2350 CD2 PHE 346 15.145 6.057 40.222 1.00 24.17 1DLC2474 ATOM 2351 CE1 PHE 346 16.884 5.863 38.079 1.00 26.24 1DLC2475 ATOM 2352 CE2 PHE 346 14.726 5.457 39.037 1.00 22.53 1DLC2476 ATOM 2353 CZ PHE 346 15.594 5.359 37.966 1.00 22.75 1DLC2477 ATOM 2354 N GLN 347 16.365 9.747 39.452 1.00 26.19 1DLC2478 ATOM 2355 CA GLN 347 15.361 10.368 38.602 1.00 28.50 1DLC2479 ATOM 2356 C GLN 347 15.031 9.390 37.497 1.00 29.83 1DLC2480 ATOM 2357 O GLN 347 15.876 9.075 36.649 1.00 29.71 1DLC2481 ATOM 2358 CB GLN 347 15.840 11.692 38.001 1.00 30.26 1DLC2482 ATOM 2359 CG GLN 347 14.880 12.280 36.951 1.00 29.03 1DLC2483 ATOM 2360 CD GLN 347 13.454 12.473 37.471 1.00 31.21 1DLC2484 ATOM 2361 OE1 GLN 347 13.234 13.083 38.515 1.00 31.71 1DLC2485 ATOM 2362 NE2 GLN 347 12.482 11.949 36.739 1.00 34.89 1DLC2486 ATOM 2363 N PRO 348 13.816 8.831 37.537 1.00 29.99 1DLC2487 ATOM 2364 CA PRO 348 13.392 7.873 36.521 1.00 30.56 1DLC2488 ATOM 2365 C PRO 348 13.079 8.512 35.180 1.00 31.08 1DLC2489 ATOM 2366 O PRO 348 12.571 9.630 35.109 1.00 29.47 1DLC2490 ATOM 2367 CB PRO 348 12.148 7.249 37.146 1.00 30.82 1DLC2491 ATOM 2368 CG PRO 348 11.586 8.367 37.960 1.00 28.95 1DLC2492 ATOM 2369 CD PRO 348 12.814 8.934 38.613 1.00 28.01 1DLC2493 ATOM 2370 N GLY 349 13.494 7.835 34.122 1.00 32.08 1DLC2494 ATOM 2371 CA GLY 349 13.203 8.310 32.788 1.00 36.84 1DLC2495 ATOM 2372 C GLY 349 11.906 7.627 32.382 1.00 40.08 1DLC2496 ATOM 2373 O GLY 349 11.629 6.511 32.825 1.00 39.90 1DLC2497 ATOM 2374 N TYR 350 11.103 8.277 31.550 1.00 42.86 1DLC2498 ATOM 2375 CA TYR 350 9.836 7.697 31.119 1.00 42.49 1DLC2499 ATOM 2376 C TYR 350 9.976 6.282 30.548 1.00 42.42 1DLC2500 ATOM 2377 O TYR 350 9.096 5.447 30.742 1.00 38.59 1DLC2501 ATOM 2378 CB TYR 350 9.157 8.611 30.107 1.00 41.54 1DLC2502 ATOM 2379 CG TYR 350 7.723 8.243 29.846 1.00 42.11 1DLC2503 ATOM 2380 CD1 TYR 350 6.758 8.372 30.846 1.00 42.70 1DLC2504 ATOM 2381 CD2 TYR 350 7.323 7.778 28.597 1.00 41.41 1DLC2505 ATOM 2382 CE1 TYR 350 5.428 8.051 30.604 1.00 43.17 1DLC2506 ATOM 2383 CE2 TYR 350 6.002 7.453 28.345 1.00 44.30 1DLC2507 ATOM 2384 CZ TYR 350 5.060 7.594 29.350 1.00 44.01 1DLC2508 ATOM 2385 OH TYR 350 3.751 7.285 29.084 1.00 51.17 1DLC2509 ATOM 2386 N TYR 351 11.091 6.013 29.870 1.00 46.30 1DLC2510 ATOM 2387 CA TYR 351 11.342 4.689 29.293 1.00 49.39 1DLC2511 ATOM 2388 C TYR 351 12.413 3.853 30.005 1.00 50.19 1DLC2512 ATOM 2389 O TYR 351 12.900 2.862 29.459 1.00 49.12 1DLC2513 ATOM 2390 CB TYR 351 11.660 4.807 27.805 1.00 52.75 1DLC2514 ATOM 2391 CG TYR 351 10.484 5.296 27.001 1.00 59.62 1DLC2515 ATOM 2392 CD1 TYR 351 9.431 4.437 26.674 1.00 60.34 1DLC2516 ATOM 2393 CD2 TYR 351 10.401 6.629 26.596 1.00 62.29 1DLC2517 ATOM 2394 CE1 TYR 351 8.324 4.896 25.964 1.00 62.98 1DLC2518 ATOM 2395 CE2 TYR 351 9.299 7.101 25.888 1.00 64.82 1DLC2519 ATOM 2396 CZ TYR 351 8.263 6.231 25.577 1.00 66.21 1DLC2520 ATOM 2397 OH TYR 351 7.167 6.710 24.891 1.00 71.16 1DLC2521 ATOM 2398 N GLY 352 12.764 4.247 31.229 1.00 51.80 1DLC2522 ATOM 2399 CA GLY 352 13.756 3.519 32.013 1.00 54.02 1DLC2523 ATOM 2400 C GLY 352 15.203 3.694 31.585 1.00 54.76 1DLC2524 ATOM 2401 O GLY 352 16.086 3.933 32.407 1.00 56.76 1DLC2525 ATOM 2402 N ASN 353 15.439 3.562 30.289 1.00 54.09 1DLC2526 ATOM 2403 CA ASN 353 16.768 3.700 29.702 1.00 54.37 1DLC2527 ATOM 2404 C ASN 353 17.383 5.096 29.857 1.00 52.91 1DLC2528 ATOM 2405 O ASN 353 18.599 5.253 29.836 1.00 53.09 1DLC2529 ATOM 2406 CB ASN 353 16.685 3.347 28.216 1.00 58.15 1DLC2530 ATOM 2407 CG ASN 353 15.459 3.949 27.538 1.00 61.25 1DLC2531 ATOM 2408 OD1 ASN 353 15.047 5.069 27.845 1.00 63.28 1DLC2532 ATOM 2409 ND2 ASN 353 14.855 3.194 26.635 1.00 64.45 1DLC2533 ATOM 2410 N ASP 354 16.528 6.097 30.021 1.00 50.29 1DLC2534 ATOM 2411 CA ASP 354 16.961 7.488 30.140 1.00 46.56 1DLC2535 ATOM 2412 C ASP 354 17.013 8.056 31.560 1.00 45.20 1DLC2536 ATOM 2413 D ASP 354 16.987 9.277 31.759 1.00 41.77 1DLC2537 ATOM 2414 CB ASP 354 16.062 8.362 29.269 1.00 47.89 1DLC2538 ATOM 2415 CG ASP 354 14.594 8.263 29.652 1.00 49.69 1DLC2539 ATOM 2416 OD1 ASP 354 14.110 7.156 29.988 1.00 49.83 1DLC2540 ATOM 2417 OD2 ASP 354 13.921 9.309 29.616 1.00 53.54 1DLC2541 ATOM 2418 N SER 355 17.088 7.170 32.545 1.00 42.98 1DLC2542 ATOM 2419 CA SER 355 17.141 7.582 33.946 1.00 42.29 1DLC2543 ATOM 2420 C SER 355 18.522 8.087 34.354 1.00 39.61 1DLC2544 ATOM 2421 O SER 355 19.501 7.891 33.636 1.00 40.89 1DLC2545 ATOM 2422 CB SER 355 16.752 6.407 34.837 1.00 45.53 1DLC2546 ATOM 2423 OG SER 355 15.491 5.879 34.453 1.00 49.12 1DLC2547 ATOM 2424 N PHE 356 18.595 8.753 35.500 1.00 35.84 1DLC2548 ATOM 2425 CA PHE 356 19.863 9.268 36.013 1.00 33.36 1DLC2549 ATOM 2426 C PHE 356 19.735 9.633 37.486 1.00 33.41 1DLC2550 ATOM 2427 O PHE 356 18.626 9.773 38.006 1.00 33.51 1DLC2551 ATOM 2428 CB PHE 356 20.358 10.484 35.200 1.00 30.78 1DLC2552 ATOM 2429 CG PHE 356 19.510 11.727 35.353 1.00 30.29 1DLC2553 ATOM 2430 CD1 PHE 356 18.374 11.921 34.568 1.00 30.93 1DLC2554 ATOM 2431 CD2 PHE 356 19.849 12.709 36.278 1.00 29.49 1DLC2555 ATOM 2432 CE1 PHE 356 17.592 13.073 34.708 1.00 27.44 1DLC2556 ATOM 2433 CE2 PHE 356 19.071 13.864 36.424 1.00 26.60 1DLC2557 ATOM 2434 CZ PHE 356 17.946 14.044 35.640 1.00 27.20 1DLC2558 ATOM 2435 N ASN 357 20.864 9.665 38.183 1.00 34.56 1DLC2559 ATOM 2436 CA ASN 357 20.883 10.051 39.594 1.00 34.66 1DLC2560 ATOM 2437 C ASN 357 21.299 11.510 39.637 1.00 31.40 1DLC2561 ATOM 2438 O ASN 357 21.977 11.990 38.726 1.00 30.66 1DLC2562 ATOM 2439 CB ASN 357 21.892 9.221 40.385 1.00 38.51 1DLC2563 ATOM 2440 CG ASN 357 21.411 7.816 40.658 1.00 40.71 1DLC2564 ATOM 2441 OD1 ASN 357 22.211 6.921 40.897 1.00 45.00 1DLC2565 ATOM 2442 ND2 ASN 357 20.103 7.611 40.629 1.00 42.48 1DLC2566 ATOM 2443 N TYR 358 20.923 12.219 40.688 1.00 27.67 1DLC2567 ATOM 2444 CA TYR 358 21.294 13.620 40.758 1.00 26.55 1DLC2568 ATOM 2445 C TYR 358 21.457 14.115 42.186 1.00 26.59 1DLC2569 ATOM 2446 O TYR 358 20.937 13.521 43.132 1.00 24.94 1DLC2570 ATOM 2447 CB TYR 358 20.272 14.483 39.999 1.00 25.94 1DLC2571 ATOM 2448 CG TYR 358 18.936 14.556 40.683 1.00 27.85 1DLC2572 ATOM 2449 CD1 TYR 358 17.962 13.584 40.461 1.00 31.47 1DLC2573 ATOM 2450 CD2 TYR 358 18.679 15.546 41.630 1.00 32.37 1DLC2574 ATOM 2451 CE1 TYR 358 16.765 13.587 41.180 1.00 34.73 1DLC2575 ATOM 2452 CE2 TYR 358 17.494 15.562 42.354 1.00 36.61 1DLC2576 ATOM 2453 CZ TYR 358 16.541 14.581 42.131 1.00 38.10 1DLC2577 ATOM 2454 OH TYR 358 15.384 14.586 42.886 1.00 45.04 1DLC2578 ATOM 2455 N TRP 359 22.212 15.200 42.318 1.00 27.94 1DLC2579 ATOM 2456 CA TRP 359 22.487 15.852 43.596 1.00 26.27 1DLC2580 ATOM 2457 C TRP 359 21.183 16.510 44.063 1.00 24.40 1DLC2581 ATOM 2458 O TRP 359 20.694 17.462 43.449 1.00 25.89 1DLC2582 ATOM 2459 CB TRP 359 23.596 16.890 43.382 1.00 23.83 1DLC2583 ATOM 2460 CG TRP 359 24.070 17.584 44.604 1.00 24.65 1DLC2584 ATOM 2461 CD1 TRP 359 23.782 17.267 45.901 1.00 25.90 1DLC2585 ATOM 2462 CD2 TRP 359 24.919 18.733 44.649 1.00 25.70 1DLC2586 ATOM 2463 NE1 TRP 359 24.396 18.152 46.752 1.00 25.43 1DLC2587 ATOM 2464 CE2 TRP 359 25.103 19.062 46.011 1.00 27.53 1DLC2588 ATOM 2465 CE3 TRP 359 25.547 19.518 43.669 1.00 26.62 1DLC2589 ATOM 2466 CZ2 TRP 359 25.894 20.147 46.419 1.00 27.25 1DLC2590 ATOM 2467 CZ3 TRP 359 26.333 20.596 44.075 1.00 25.15 1DLC2591 ATOM 2468 CH2 TRP 359 26.498 20.897 45.437 1.00 26.00 1DLC2592 ATOM 2469 N SER 360 20.610 15.977 45.132 1.00 22.69 1DLC2593 ATOM 2470 CA SER 360 19.339 16.473 45.654 1.00 23.95 1DLC2594 ATOM 2471 C SER 360 19.405 17.470 46.812 1.00 25.02 1DLC2595 ATOM 2472 O SER 360 18.520 18.317 46.966 1.00 26.55 1DLC2596 ATOM 2473 CB SER 360 18.460 15.289 46.060 1.00 22.05 1DLC2597 ATOM 2474 OG SER 360 19.050 14.555 47.123 1.00 20.36 1DLC2598 ATOM 2475 N GLY 361 20.422 17.345 47.653 1.00 23.75 1DLC2599 ATOM 2476 CA GLY 361 20.542 18.246 48.782 1.00 21.17 1DLC2600 ATOM 2477 C GLY 361 21.935 18.193 49.361 1.00 24.69 1DLC2601 ATOM 2478 O GLY 361 22.789 17.443 48.871 1.00 26.41 1DLC2602 ATOM 2479 N ASN 362 22.181 18.955 50.419 1.00 22.30 1DLC2603 ATOM 2480 CA ASN 362 23.510 18.954 51.003 1.00 22.20 1DLC2604 ATOM 2481 C ASN 362 23.590 19.569 52.381 1.00 21.51 1DLC2605 ATOM 2482 O ASN 362 22.643 20.179 52.871 1.00 20.57 1DLC2606 ATOM 2483 CB ASN 362 24.485 19.713 50.089 1.00 24.04 1DLC2607 ATOM 2484 CG ASN 362 24.420 21.228 50.291 1.00 28.34 1DLC2608 ATOM 2485 OD1 ASN 362 25.165 21.789 51.088 1.00 28.65 1DLC2609 ATOM 2486 ND2 ASN 362 23.516 21.885 49.593 1.00 26.03 1DLC2610 ATOM 2487 N TYR 363 24.743 19.346 52.993 1.00 24.00 1DLC2611 ATOM 2488 CA TYR 363 25.118 19.902 54.286 1.00 26.62 1DLC2612 ATOM 2489 C TYR 363 26.466 20.551 53.960 1.00 28.28 1DLC2613 ATOM 2490 O TYR 363 27.191 20.085 53.067 1.00 27.60 1DLC2614 ATOM 2491 CB TYR 363 25.381 18.810 55.329 1.00 27.58 1DLC2615 ATOM 2492 CG TYR 363 24.178 18.317 56.087 1.00 28.34 1DLC2616 ATOM 2493 CD1 TYR 363 23.515 19.138 56.997 1.00 29.04 1DLC2617 ATOM 2494 CD2 TYR 363 23.719 17.016 55.915 1.00 30.38 1DLC2618 ATOM 2495 CE1 TYR 363 22.425 18.672 57.718 1.00 32.23 1DLC2619 ATOM 2496 CE2 TYR 363 22.630 16.537 56.628 1.00 33.13 1DLC2620 ATOM 2497 CZ TYR 363 21.985 17.366 57.529 1.00 34.94 1DLC2621 ATOM 2498 OH TYR 363 20.902 16.876 58.232 1.00 36.70 1DLC2622 ATOM 2499 N VAL 364 26.791 21.640 54.641 1.00 28.34 1DLC2623 ATOM 2500 CA VAL 364 28.075 22.294 54.431 1.00 26.27 1DLC2624 ATOM 2501 C VAL 364 28.651 22.630 55.790 1.00 24.54 1DLC2625 ATOM 2502 O VAL 364 27.923 22.972 56.722 1.00 27.34 1DLC2626 ATOM 2503 CB VAL 364 27.957 23.592 53.612 1.00 28.72 1DLC2627 ATOM 2504 CG1 VAL 364 29.333 24.079 53.197 1.00 30.77 1DLC2628 ATOM 2505 CG2 VAL 364 27.135 23.356 52.393 1.00 36.32 1DLC2629 ATOM 2506 N SER 365 29.953 22.456 55.920 1.00 24.40 1DLC2630 ATOM 2507 CA SER 365 30.639 22.766 57.166 1.00 24.54 1DLC2631 ATOM 2508 C SER 365 31.804 23.688 56.850 1.00 23.42 1DLC2632 ATOM 2509 O SER 365 32.538 23.477 55.883 1.00 21.82 1DLC2633 ATOM 2510 CB SER 365 31.166 21.496 57.845 1.00 27.44 1DLC2634 ATOM 2511 OG SER 365 30.117 20.716 58.400 1.00 34.19 1DLC2635 ATOM 2512 N THR 366 31.938 24.737 57.645 1.00 21.84 1DLC2636 ATOM 2513 CA THR 366 33.018 25.690 57.469 1.00 23.59 1DLC2637 ATOM 2514 C THR 366 33.789 25.846 58.767 1.00 24.57 1DLC2638 ATOM 2515 O THR 366 33.265 25.580 59.851 1.00 21.97 1DLC2639 ATOM 2516 CB THR 366 32.502 27.105 57.062 1.00 22.30 1DLC2640 ATOM 2517 OG1 THR 366 31.532 27.558 58.015 1.00 21.18 1DLC2641 ATOM 2518 CG2 THR 366 31.913 27.107 55.641 1.00 16.40 1DLC2642 ATOM 2519 N ARG 367 35.060 26.198 58.654 1.00 23.86 1DLC2643 ATOM 2520 CA ARG 367 35.843 26.439 59.849 1.00 26.59 1DLC2644 ATOM 2521 C ARG 367 35.989 27.960 59.945 1.00 25.50 1DLC2645 ATOM 2522 O ARG 367 36.029 28.663 58.923 1.00 23.82 1DLC2646 ATOM 2523 CB ARG 367 37.201 25.721 59.819 1.00 28.50 1DLC2647 ATOM 2524 CG ARG 367 38.231 26.244 58.838 1.00 33.38 1DLC2648 ATOM 2525 CD ARG 367 39.617 26.227 59.483 1.00 39.84 1DLC2649 ATOM 2526 NE ARG 367 39.715 27.236 60.538 1.00 46.62 1DLC2650 ATOM 2527 CZ ARG 367 40.452 27.122 61.642 1.00 47.81 1DLC2651 ATOM 2528 NH1 ARG 367 41.174 26.027 61.857 1.00 49.54 1DLC2652 ATOM 2529 NH2 ARG 367 40.473 28.114 62.528 1.00 42.81 1DLC2653 ATOM 2530 N PRO 368 35.927 28.497 61.167 1.00 25.39 1DLC2654 ATOM 2531 CA PRO 368 36.055 29.944 61.357 1.00 24.95 1DLC2655 ATOM 2532 C PRO 368 37.430 30.514 61.038 1.00 25.37 1DLC2656 ATOM 2533 O PRO 368 38.312 29.832 60.517 1.00 25.73 1DLC2657 ATOM 2534 CB PRO 368 35.695 30.131 62.833 1.00 23.10 1DLC2658 ATOM 2535 CG PRO 368 36.052 28.813 63.453 1.00 27.44 1DLC2659 ATOM 2536 CD PRO 368 35.568 27.826 62.427 1.00 25.33 1DLC2660 ATOM 2537 N SER 369 37.582 31.800 61.301 1.00 25.94 1DLC2661 ATOM 2538 CA SER 369 38.849 32.470 61.075 1.00 28.16 1DLC2662 ATOM 2539 C SER 369 39.857 31.953 62.126 1.00 30.36 1DLC2663 ATOM 2540 O SER 369 39.459 31.446 63.195 1.00 27.15 1DLC2664 ATOM 2541 CB SER 369 38.647 33.983 61.205 1.00 28.25 1DLC2665 ATOM 2542 OG SER 369 39.797 34.702 60.811 1.00 31.44 1DLC2666 ATOM 2543 N ILE 370 41.151 32.051 61.813 1.00 27.89 1DLC2667 ATOM 2544 CA ILE 370 42.198 31.602 62.731 1.00 26.08 1DLC2668 ATOM 2545 C ILE 370 41.936 32.085 64.169 1.00 25.65 1DLC2669 ATOM 2546 O ILE 370 41.477 33.208 64.388 1.00 24.58 1DLC2670 ATOM 2547 CB ILE 370 43.612 32.047 62.241 1.00 28.63 1DLC2671 ATOM 2548 CG1 ILE 370 44.695 31.410 63.116 1.00 28.81 1DLC2672 ATOM 2549 CG2 ILE 370 43.749 33.576 62.236 1.00 24.11 1DLC2673 ATOM 2550 CD1 ILE 370 46.064 31.482 62.521 1.00 22.91 1DLC2674 ATOM 2551 N GLY 371 42.179 31.218 65.143 1.00 26.12 1DLC2675 ATOM 2552 CA GLY 371 41.934 31.588 66.526 1.00 27.59 1DLC2676 ATOM 2553 C GLY 371 40.831 30.742 67.132 1.00 31.60 1DLC2677 ATOM 2554 O GLY 371 40.728 30.608 68.347 1.00 32.87 1DLC2678 ATOM 2555 N SER 372 39.973 30.198 66.279 1.00 34.07 1DLC2679 ATOM 2556 CA SER 372 38.886 29.334 66.733 1.00 38.39 1DLC2680 ATOM 2557 C SER 372 38.918 28.050 65.926 1.00 42.67 1DLC2681 ATOM 2558 O SER 372 39.225 28.058 64.731 1.00 45.63 1DLC2682 ATOM 2559 CB SER 372 37.522 30.000 66.553 1.00 37.68 1DLC2683 ATOM 2560 OG SER 372 36.484 29.117 66.945 1.00 35.42 1DLC2684 ATOM 2561 N ASN 373 38.605 26.940 66.571 1.00 45.05 1DLC2685 ATOM 2562 CA ASN 373 38.624 25.669 65.869 1.00 49.01 1DLC2686 ATOM 2563 C ASN 373 37.271 24.961 65.761 1.00 49.16 1DLC2687 ATOM 2564 O ASN 373 37.158 23.940 65.078 1.00 50.24 1DLC2688 ATOM 2565 CB ASN 373 39.670 24.745 66.501 1.00 53.82 1DLC2689 ATOM 2566 CG ASN 373 41.091 25.214 66.246 1.00 58.42 1DLC2690 ATOM 2567 OD1 ASN 373 41.791 25.640 67.163 1.00 62.66 1DLC2691 ATOM 2568 ND2 ASN 373 41.523 25.148 64.992 1.00 60.46 1DLC2692 ATOM 2569 N ASP 374 36.239 25.502 66.403 1.00 47.14 1DLC2693 ATOM 2570 CA ASP 374 34.941 24.849 66.331 1.00 48.54 1DLC2694 ATOM 2571 C ASP 374 34.255 25.010 64.975 1.00 45.07 1DLC2695 ATOM 2572 O ASP 374 33.989 26.120 64.514 1.00 43.01 1DLC2696 ATOM 2573 CB ASP 374 34.028 25.232 67.506 1.00 55.25 1DLC2697 ATOM 2574 CG ASP 374 33.826 26.723 67.644 1.00 62.12 1DLC2698 ATOM 2575 OD1 ASP 374 33.068 27.308 66.835 1.00 68.28 1DLC2699 ATOM 2576 OD2 ASP 374 34.403 27.303 68.590 1.00 66.38 1DLC2700 ATOM 2577 N ILE 375 34.029 23.868 64.335 1.00 41.73 1DLC2701 ATOM 2578 CA ILE 375 33.408 23.776 63.020 1.00 37.95 1DLC2702 ATOM 2579 C ILE 375 31.921 24.131 63.008 1.00 36.63 1DLC2703 AT6M 2580 O ILE 375 31.143 23.638 63.816 1.00 38.76 1DLC2704 ATOM 2581 CB ILE 375 33.618 22.355 62.428 1.00 36.39 1DLC2705 ATOM 2582 CG1 ILE 375 35.110 22.015 62.422 1.00 36.11 1DLC2706 ATOM 2583 CG2 ILE 375 33.056 22.254 61.014 1.00 35.62 1DLC2707 ATOM 2584 CD1 ILE 375 35.966 22.993 61.658 1.00 34.10 1DLC2708 ATOM 2585 N ILE 376 31.541 25.001 62.084 1.00 35.72 1DLC2709 ATOM 2586 CA ILE 376 30.156 25.428 61.942 1.00 31.79 1DLC2710 ATOM 2587 C ILE 376 29.478 24.575 60.883 1.00 31.77 1DLC2711 ATOM 2588 O ILE 376 29.948 24.483 59.751 1.00 32.62 1DLC2712 ATOM 2589 CB ILE 376 30.077 26.885 61.481 1.00 31.87 1DLC2713 ATOM 2590 CG1 ILE 376 30.864 27.781 62.432 1.00 27.90 1DLC2714 ATOM 2591 CG2 ILE 376 28.632 27.324 61.391 1.00 28.10 1DLC2715 ATOM 2592 CD1 ILE 376 31.122 29.148 61.868 1.00 30.02 1DLC2716 ATOM 2593 N THR 377 28.390 23.921 61.250 1.00 31.76 1DLC2717 ATOM 2594 CA THR 377 27.696 23.104 60.275 1.00 31.91 1DLC2718 ATOM 2595 C THR 377 26.337 23.687 59.972 1.00 31.49 1DLC2719 ATOM 2596 O THR 377 25.590 24.070 60.872 1.00 32.65 1DLC2720 ATOM 2597 CB THR 377 27.577 21.653 60.711 1.00 32.50 1DLC2721 ATOM 2598 OG1 THR 377 28.890 21.137 60.960 1.00 34.88 1DLC2722 ATOM 2599 CG2 THR 377 26.937 20.833 59.601 1.00 36.51 1DLC2723 ATOM 2600 N SER 378 26.056 23.790 58.681 1.00 31.02 1DLC2724 ATOM 2601 CA SER 378 24.813 24.351 58.166 1.00 30.69 1DLC2725 ATOM 2602 C SER 378 23.570 23.484 58.326 1.00 30.61 1DLC2726 ATOM 2603 O SER 378 23.648 22.276 58.573 1.00 32.66 1DLC2727 ATOM 2604 CB SER 378 24.969 24.591 56.672 1.00 29.80 1DLC2728 ATOM 2605 OG SER 378 24.957 23.342 56.002 1.00 24.82 1DLC2729 ATOM 2606 N PRO 379 22.392 24.105 58.200 1.00 30.39 1DLC2730 ATOM 2607 CA PRO 379 21.155 23.332 58.313 1.00 29.82 1DLC2731 ATOM 2608 C PRO 379 21.130 22.476 57.042 1.00 29.81 1DLC2732 ATOM 2609 O PRO 379 21.967 22.660 56.154 1.00 31.85 1DLC2733 ATOM 2610 CB PRO 379 20.076 24.413 58.234 1.00 28.69 1DLC2734 ATOM 2611 CG PRO 379 20.761 25.632 58.763 1.00 29.56 1DLC2735 ATOM 2612 CD PRO 379 22.107 25.547 58.115 1.00 30.05 1DLC2736 ATOM 2613 N PHE 380 20.206 21.535 56.941 1.00 28.23 1DLC2737 ATOM 2614 CA PHE 380 20.154 20.740 55.727 1.00 27.04 1DLC2738 ATOM 2615 C PHE 380 19.513 21.568 54.606 1.00 26.98 1DLC2739 ATOM 2616 O PHE 380 18.578 22.335 54.850 1.00 29.48 1DLC2740 ATOM 2617 CB PHE 380 19.381 19.435 55.938 1.00 25.05 1DLC2741 ATOM 2618 CG PHE 380 19.383 18.545 54.731 1.00 24.11 1DLC2742 ATOM 2619 CD1 PHE 380 20.527 17.846 54.377 1.00 20.89 1DLC2743 ATOM 2620 CD2 PHE 380 18.268 18.467 53.903 1.00 21.40 1DLC2744 ATOM 2621 CE1 PHE 380 20.566 17.089 53.216 1.00 20.66 1DLC2745 ATOM 2622 CE2 PHE 380 18.300 17.714 52.742 1.00 22.67 1DLC2746 ATOM 2623 CZ PHE 380 19.453 17.025 52.396 1.00 21.89 1DLC2747 ATOM 2624 N TYR 381 20.050 21.446 53.395 1.00 26.14 1DLC2748 ATOM 2625 CA TYR 381 19.525 22.167 52.241 1.00 25.56 1DLC2749 ATOM 2626 C TYR 381 19.056 21.183 51.182 1.00 28.82 1DLC2750 ATOM 2627 O TYR 381 19.812 20.291 50.797 1.00 31.78 1DLC2751 ATOM 2628 CB TYR 381 20.607 23.053 51.608 1.00 25.41 1DLC2752 ATOM 2629 CG TYR 381 21.187 24.117 52.512 1.00 25.18 1DLC2753 ATOM 2630 CD1 TYR 381 20.375 25.090 53.087 1.00 23.16 1DLC2754 ATOM 2631 CD2 TYR 381 22.558 24.162 52.779 1.00 21.71 1DLC2755 ATOM 2632 CE1 TYR 381 20.914 26.080 53.905 1.00 24.57 1DLC2756 ATOM 2633 CE2 TYR 381 23.101 25.148 53.592 1.00 20.00 1DLC2757 ATOM 2634 CZ TYR 381 22.277 26.102 54.153 1.00 20.22 1DLC2758 ATOM 2635 OH TYR 381 22.797 27.071 54.980 1.00 21.73 1DLC2759 ATOM 2636 N GLY 382 17.828 21.358 50.696 1.00 30.75 1DLC2760 ATOM 2637 CA GLY 382 17.307 20.495 49.646 1.00 29.98 1DLC2761 ATOM 2638 C GLY 382 16.603 19.230 50.093 1.00 32.07 1DLC2762 ATOM 2639 O GLY 382 15.939 19.219 51.126 1.00 34.65 1DLC2763 ATOM 2640 N ASN 383 16.765 18.157 49.325 1.00 31.65 1DLC2764 ATOM 2641 CA ASN 383 16.123 16.877 49.632 1.00 31.34 1DLC2765 ATOM 2642 C ASN 383 17.023 15.758 50.136 1.00 29.92 1DLC2766 ATOM 2643 O ASN 383 18.083 15.493 49.567 1.00 28.55 1DLC2767 ATOM 2644 CB ASN 383 15.346 16.373 48.417 1.00 32.90 1DLC2768 ATOM 2645 CG ASN 383 13.928 16.892 48.383 1.00 33.10 1DLC2769 ATOM 2646 OD1 ASN 383 13.267 16.978 49.412 1.00 34.94 1DLC2770 ATOM 2647 ND2 ASN 383 13.453 17.242 47.203 1.00 33.54 1DLC2771 ATOM 2648 N LYS 384 16.566 15.070 51.179 1.00 30.21 1DLC2772 ATOM 2649 CA LYS 384 17.318 13.959 51.755 1.00 30.37 1DLC2773 ATOM 2650 C LYS 384 17.691 12.931 50.696 1.00 29.47 1DLC2774 ATOM 2651 O LYS 384 17.039 12.806 49.666 1.00 30.67 1DLC2775 ATOM 2652 CB LYS 384 16.538 13.283 52.877 1.00 31.48 1DLC2776 ATOM 2653 CG LYS 384 16.309 14.156 54.090 1.00 37.12 1DLC2777 ATOM 2654 CD LYS 384 17.594 14.459 54.835 1.00 36.68 1DLC2778 ATOM 2655 CE LYS 384 17.275 15.123 56.166 1.00 43.15 1DLC2779 ATOM 2656 NZ LYS 384 18.485 15.319 57.010 1.00 50.78 1DLC2780 ATOM 2657 N SER 385 18.736 12.174 50.977 1.00 31.31 1DLC2781 ATOM 2658 CA SER 385 19.230 11.191 50.033 1.00 33.17 1DLC2782 ATOM 2659 C SER 385 18.391 9.923 49.935 1.00 34.75 1DLC2783 ATOM 2660 O SER 385 17.817 9.464 50.921 1.00 35.39 1DLC2784 ATOM 2661 CB SER 385 20.672 10.821 50.401 1.00 31.08 1DLC2785 ATOM 2662 OG SER 385 21.444 10.511 49.254 1.00 29.79 1DLC2786 ATOM 2663 N SER 386 18.249 9.425 48.714 1.00 36.92 1DLC2787 ATOM 2664 CA SER 386 17.559 8.158 48.476 1.00 39.89 1DLC2788 ATOM 2665 C SER 386 18.713 7.175 48.234 1.00 41.41 1DLC2789 ATOM 2666 O SER 386 18.573 5.965 48.395 1.00 45.84 1DLC2790 ATOM 2667 CB SER 386 16.666 8.215 47.233 1.00 38.56 1DLC2791 ATOM 2668 OG SER 386 17.424 8.118 46.036 1.00 38.63 1DLC2792 ATOM 2669 N GLU 387 19.862 7.730 47.857 1.00 39.62 1DLC2793 ATOM 2670 CA GLU 387 21.067 6.957 47.593 1.00 38.96 1DLC2794 ATOM 2671 C GLU 387 22.112 7.171 48.694 1.00 37.55 1DLC2795 ATOM 2672 O GLU 387 21.908 7.960 49.618 1.00 37.34 1DLC2796 ATOM 2673 CB GLU 387 21.653 7.387 46.250 1.00 41.28 1DLC2797 ATOM 2674 CG GLU 387 20.667 7.310 45.114 1.00 48.83 1DLC2798 ATOM 2675 CD GLU 387 19.985 5.962 45.046 1.00 54.03 1DLC2799 ATOM 2676 OE1 GLU 387 20.706 4.937 45.061 1.00 55.83 1DLC2800 ATOM 2677 OE2 GLU 387 18.732 5.928 44.997 1.00 55.98 1DLC2801 ATOM 2678 N PRO 388 23.230 6.438 48.632 1.00 36.30 1DLC2802 ATOM 2679 CA PRO 388 24.279 6.593 49.645 1.00 35.40 1DLC2803 ATOM 2680 C PRO 388 24.950 7.981 49.624 1.00 34.68 1DLC2804 ATOM 2681 O PRO 388 25.396 8.486 48.603 1.00 33.48 1DLC2805 ATOM 2682 CB PRO 388 25.278 5.503 49.261 1.00 35.55 1DLC2806 ATOM 2683 CG PRO 388 24.406 4.448 48.677 1.00 36.31 1DLC2807 ATOM 2684 CD PRO 388 23.481 5.245 47.804 1.00 35.19 1DLC2808 ATOM 2685 N VAL 389 25.025 8.573 50.826 1.00 31.70 1DLC2809 ATOM 2686 CA VAL 389 25.640 9.878 51.034 1.00 33.25 1DLC2810 ATOM 2687 C VAL 389 27.136 9.922 50.661 1.00 34.25 1DLC2811 ATOM 2688 O VAL 389 27.852 8.928 50.800 1.00 35.26 1DLC2812 ATOM 2689 CB VAL 389 25.459 10.293 52.516 1.00 31.82 1DLC2813 ATOM 2690 CG1 VAL 389 26.378 11.431 52.887 1.00 34.96 1DLC2814 ATOM 2691 CG2 VAL 389 24.021 10.687 52.761 1.00 34.70 1DLC2815 ATOM 2692 N GLN 390 27.589 11.069 50.159 1.00 34.02 1DLC2816 ATOM 2693 CA GLN 390 28.994 11.268 49.798 1.00 34.03 1DLC2817 ATOM 2694 C GLN 390 29.556 12.458 50.567 1.00 34.94 1DLC2818 ATOM 2695 O GLN 390 28.929 13.511 50.642 1.00 37.45 1DLC2819 ATOM 2696 CB GLN 390 29.156 11.502 48.298 1.00 30.86 1DLC2820 ATOM 2697 CG GLN 390 28.968 10.258 47.478 1.00 34.90 1DLC2821 ATOM 2698 CD GLN 390 28.993 10.520 45.985 1.00 37.84 1DLC2822 ATOM 2699 OE1 GLN 390 29.887 11.189 45.467 1.00 39.97 1DLC2823 ATOM 2700 NE2 GLN 390 28.011 9.982 45.282 1.00 36.71 1DLC2824 ATOM 2701 N ASN 391 30.735 12.285 51.150 1.00 36.13 1DLC2825 ATOM 2702 CA ASN 391 31.364 13.350 51.918 1.00 35.90 1DLC2826 ATOM 2703 C ASN 391 32.749 13.684 51.399 1.00 34.56 1DLC2827 ATOM 2704 O ASN 391 33.568 12.796 51.197 1.00 36.19 1DLC2828 ATOM 2705 CB ASN 391 31.471 12.951 53.389 1.00 38.72 1DLC2829 ATOM 2706 CG ASN 391 30.122 12.680 54.021 1.00 46.12 1DLC2830 ATOM 2707 OD1 ASN 391 29.101 13.193 53.576 1.00 54.69 1DLC2831 ATOM 2708 ND2 LEU 392 30.108 11.871 55.065 1.00 48.42 1DLC2832 ATOM 2709 N LEU 392 32.992 14.965 51.149 1.00 35.38 1DLC2833 ATOM 2710 CA LEU 392 34.302 15.428 50.690 1.00 31.94 1DLC2834 ATOM 2711 C LEU 392 34.846 16.361 51.758 1.00 32.63 1DLC2835 ATOM 2712 O LEU 392 34.106 17.196 52.280 1.00 35.13 1DLC2836 ATOM 2713 CB LEU 392 34.192 16.194 49.369 1.00 27.68 1DLC2837 ATOM 2714 CG LEU 392 33.624 15.448 48.164 1.00 26.82 1DLC2838 ATOM 2715 CD1 LEU 392 33.756 16.283 46.906 1.00 26.78 1DLC2839 ATOM 2716 CD2 LEU 392 34.365 14.155 47.987 1.00 29.40 1DLC2840 ATOM 2717 N GLU 393 36.098 16.162 52.157 1.00 34.76 1DLC2841 ATOM 2718 CA GLU 393 36.721 17.039 53.150 1.00 34.99 1DLC2842 ATOM 2719 C GLU 393 37.754 17.931 52.477 1.00 33.60 1DLC2843 ATOM 2720 O GLU 393 38.398 17.522 51.510 1.00 27.84 1DLC2844 ATOM 2721 CB GLU 393 37.371 16.246 54.273 1.00 41.28 1DLC2845 ATOM 2722 CG GLU 393 36.404 15.790 55.338 1.00 49.72 1DLC2846 ATOM 2723 CD GLU 393 36.135 14.297 55.306 1.00 57.23 1DLC2847 ATOM 2724 DE1 GLU 393 36.653 13.603 54.396 1.00 62.82 1DLC2848 ATOM 2725 OE2 GLU 393 35.401 13.814 56.200 1.00 61.57 1DLC2849 ATOM 2726 N PHE 394 37.912 19.148 52.989 1.00 35.60 1DLC2850 ATOM 2727 CA PHE 394 38.851 20.104 52.393 1.00 37.09 1DLC2851 ATOM 2728 C PHE 394 39.931 20.691 53.302 1.00 41.43 1DLC2852 ATOM 2729 O PHE 394 40.735 21.489 52.847 1.00 42.91 1DLC2853 ATOM 2730 CB PHE 394 38.069 21.238 51.721 1.00 29.33 1DLC2854 ATOM 2731 CG PHE 394 37.104 20.756 50.682 1.00 28.27 1DLC2855 ATOM 2732 CD1 PHE 394 37.521 20.549 49.369 1.00 26.99 1DLC2856 ATOM 2733 CD2 PHE 394 35.792 20.448 51.021 1.00 26.84 1DLC2857 ATOM 2734 CE1 PHE 394 36.648 20.037 48.411 1.00 24.88 1DLC2858 ATOM 2735 CE2 PHE 394 34.911 19.935 50.067 1.00 26.52 1DLC2859 ATOM 2736 CZ PHE 394 35.342 19.730 48.760 1.00 25.09 1DLC2860 ATOM 2737 N ASN 395 39.973 20.256 54.561 1.00 45.12 1DLC2861 ATOM 2738 CA ASN 395 40.939 20.741 55.563 1.00 51.55 1DLC2862 ATOM 2739 C ASN 395 42.208 21.432 55.023 1.00 53.27 1DLC2863 ATOM 2740 O ASN 395 43.197 20.769 54.699 1.00 57.04 1DLC2864 ATOM 2741 CB ASN 395 41.358 19.590 56.489 1.00 57.57 1DLC2865 ATOM 2742 CG ASN 395 40.201 18.671 56.848 1.00 64.16 1DLC2866 ATOM 2743 OD1 ASN 395 39.360 19.002 57.684 1.00 69.45 1DLC2867 ATOM 2744 ND2 ASN 395 40.144 17.516 56.202 1.00 66.55 1DLC2868 ATOM 2745 N GLY 396 42.167 22.756 54.897 1.00 52.24 1DLC2869 ATOM 2746 CA GLY 396 43.331 23.488 54.409 1.00 52.60 1DLC2870 ATOM 2747 C GLY 396 43.473 23.670 52.898 1.00 51.64 1DLC2871 ATOM 2748 O GLY 396 44.241 24.524 52.432 1.00 55.32 1DLC2872 ATOM 2749 N GLU 397 42.812 22.805 52.137 1.00 46.45 1DLC2873 ATOM 2750 CA GLU 397 42.820 22.868 50.681 1.00 40.85 1DLC2874 ATOM 2751 C GLU 397 42.048 24.096 50.190 1.00 36.96 1DLC2875 ATOM 2752 O GLU 397 41.064 24.510 50.801 1.00 36.76 1DLC2876 ATOM 2753 CB GLU 397 42.132 21.628 50.108 1.00 42.90 1DLC2877 ATOM 2754 CG GLU 397 42.655 20.311 50.629 1.00 46.38 1DLC2878 ATOM 2755 CD GLU 397 44.049 19.997 50.125 1.00 50.24 1DLC2879 ATOM 2756 OE1 GLU 397 44.319 20.217 48.920 1.00 48.15 1DLC2880 ATOM 2757 OE2 GLU 397 44.873 19.519 50.939 1.00 54.59 1DLC2881 ATOM 2758 N LYS 398 42.488 24.677 49.084 1.00 32.97 1DLC2882 ATOM 2759 CA LYS 398 41.793 25.819 48.515 1.00 29.63 1DLC2883 ATOM 2760 C LYS 398 41.163 25.405 47.194 1.00 28.78 1DLC2884 ATOM 2761 O LYS 398 41.874 25.081 46.234 1.00 28.04 1DLC2885 ATOM 2762 CB LYS 398 42.749 26.983 48.303 1.00 30.66 1DLC2886 ATOM 2763 CG LYS 398 43.278 27.560 49.591 1.00 36.26 1DLC2887 ATOM 2764 CD LYS 398 44.378 28.545 49.306 1.00 42.44 1DLC2888 ATOM 2765 CE LYS 398 44.979 29.085 50.580 1.00 44.63 1DLC2889 ATOM 2766 NZ LYS 398 46.179 29.912 50.258 1.00 52.09 1DLC2890 ATOM 2767 N VAL 399 39.830 25.374 47.162 1.00 25.99 1DLC2891 ATOM 2768 CA VAL 399 39.097 24.992 45.960 1.00 22.58 1DLC2892 ATOM 2769 C VAL 399 39.068 26.170 45.001 1.00 20.61 1DLC2893 ATOM 2770 O VAL 399 38.400 27.169 45.238 1.00 22.09 1DLC2894 ATOM 2771 CB VAL 399 37.663 24.509 46.293 1.00 24.43 1DLC2895 ATOM 2772 CG1 VAL 399 36.933 24.069 45.021 1.00 21.92 1DLC2896 ATOM 2773 CG2 VAL 399 37.726 23.355 47.281 1.00 22.57 1DLC2897 ATOM 2774 N TYR 400 39.840 26.057 43.931 1.00 19.64 1DLC2898 ATOM 2775 CA TYR 400 39.937 27.125 42.952 1.00 18.79 1DLC2899 ATOM 2776 C TYR 400 39.132 26.885 41.684 1.00 20.30 1DLC2900 ATOM 2777 O TYR 400 39.118 27.714 40.769 1.00 15.31 1DLC2901 ATOM 2778 CB TYR 400 41.408 27.404 42.624 1.00 19.27 1DLC2902 ATOM 2779 CG TYR 400 42.148 26.253 42.000 1.00 16.63 1DLC2903 ATOM 2780 CD1 TYR 400 42.774 25.290 42.791 1.00 16.65 1DLC2904 ATOM 2781 CD2 TYR 400 42.234 26.134 40.616 1.00 18.17 1DLC2905 ATOM 2782 CE1 TYR 400 43.477 24.226 42.215 1.00 19.68 1DLC2906 ATOM 2783 CE2 TYR 400 42.929 25.080 40.026 1.00 23.20 1DLC2907 ATOM 2784 CZ TYR 400 43.549 24.127 40.830 1.00 21.51 1DLC2908 ATOM 2785 OH TYR 400 44.227 23.084 40.235 1.00 22.85 1DLC2909 ATOM 2786 N ARG 401 38.461 25.742 41.632 1.00 20.95 1DLC2910 ATOM 2787 CA ARG 401 37.640 25.419 40.484 1.00 21.84 1DLC2911 ATOM 2788 C ARG 401 36.590 24.354 40.770 1.00 23.36 1DLC2912 ATOM 2789 O ARG 401 36.748 23.510 41.658 1.00 24.04 1DLC2913 ATOM 2790 CB ARG 401 38.508 24.984 39.312 1.00 24.53 1DLC2914 ATOM 2791 CG ARG 401 37.822 25.117 37.966 1.00 24.58 1DLC2915 ATOM 2792 CD ARG 401 38.656 24.464 36.894 1.00 25.33 1DLC2916 ATOM 2793 NE ARG 401 38.195 24.815 35.558 1.00 28.66 1DLC2917 ATOM 2794 CZ ARG 401 38.722 24.326 34.444 1.00 28.89 1DLC2918 ATOM 2795 NH1 ARG 401 39.724 23.463 34.506 1.00 35.25 1DLC2919 ATOM 2796 NH2 ARG 401 38.273 24.723 33.268 1.00 27.33 1DLC2920 ATOM 2797 N ALA 402 35.492 24.450 40.035 1.00 21.33 1DLC2921 ATOM 2798 CA ALA 402 34.384 23.514 40.135 1.00 21.93 1DLC2922 ATOM 2799 C ALA 402 33.763 23.383 38.747 1.00 23.71 1DLC2923 ATOM 2800 O ALA 402 33.400 24.385 38.116 1.00 27.23 1DLC2924 ATOM 2801 CB ALA 402 33.358 24.003 41.137 1.00 21.05 1DLC2925 ATOM 2802 N VAL 403 33.751 22.164 38.225 1.00 23.23 1DLC2926 ATOM 2803 CA VAL 403 33.173 21.907 36.910 1.00 24.12 1DLC2927 ATOM 2804 C VAL 403 32.056 20.874 37.081 1.00 25.85 1DLC2928 ATOM 2805 O VAL 403 32.241 19.841 37.747 1.00 26.19 1DLC2929 ATOM 2806 CB VAL 403 34.235 21.401 35.916 1.00 23.95 1DLC2930 ATOM 2807 CG1 VAL 403 33.631 21.290 34.525 1.00 19.01 1DLC2931 ATOM 2808 CG2 VAL 403 35.440 22.342 35.910 1.00 23.88 1DLC2932 ATOM 2809 N ALA 404 30.902 21.146 36.478 1.00 23.02 1DLC2933 ATOM 2810 CA ALA 404 29.754 20.263 36.631 1.00 19.31 1DLC2934 ATOM 2811 C ALA 404 29.100 19.659 35.390 1.00 18.96 1DLC2935 ATOM 2812 O ALA 404 29.104 20.236 34.299 1.00 19.34 1DLC2936 ATOM 2813 CB ALA 404 28.697 20.966 37.477 1.00 17.73 1DLC2937 ATOM 2814 N ASN 405 28.526 18.480 35.596 1.00 19.71 1DLC2938 ATOM 2815 CA ASN 405 27.792 17.748 34.574 1.00 21.57 1DLC2939 ATOM 2816 C ASN 405 26.322 17.840 34.955 1.00 21.86 1DLC2940 ATOM 2817 O ASN 405 25.963 17.847 36.143 1.00 20.98 1DLC2941 ATOM 2818 CB ASN 405 28.151 16.256 34.582 1.00 24.99 1DLC2942 ATOM 2819 CG ASN 405 29.564 15.985 34.146 1.00 28.98 1DLC2943 ATOM 2820 OD1 ASN 405 30.513 16.496 34.730 1.00 36.18 1DLC2944 ATOM 2821 ND2 ASN 405 29.720 15.150 33.136 1.00 28.22 1DLC2945 ATOM 2822 N THR 406 25.463 17.927 33.957 1.00 21.73 1DLC2946 ATOM 2823 CA THR 406 24.032 17.947 34.231 1.00 25.13 1DLC2947 ATOM 2824 C THR 406 23.374 16.983 33.257 1.00 26.31 1DLC2948 ATOM 2825 O THR 406 23.974 16.607 32.242 1.00 26.28 1DLC2949 ATOM 2826 CB THR 406 23.390 19.362 34.089 1.00 24.14 1DLC2950 ATOM 2827 OG1 THR 406 23.651 19.889 32.785 1.00 25.97 1DLC2951 ATOM 2828 CG2 THR 406 23.911 20.324 35.163 1.00 20.04 1DLC2952 ATOM 2829 N ASN 407 22.185 16.509 33.603 1.00 27.43 1DLC2953 ATOM 2830 CA ASN 407 21.474 15.608 32.706 1.00 27.11 1DLC2954 ATOM 2831 C ASN 407 19.981 15.902 32.722 1.00 25.60 1DLC2955 ATOM 2832 O ASN 407 19.478 16.551 33.637 1.00 24.05 1DLC2956 ATOM 2833 CB ASN 407 21.750 14.141 33.059 1.00 25.28 1DLC2957 ATOM 2834 CG ASN 407 21.683 13.226 31.842 1.00 22.24 1DLC2958 ATOM 2835 OD1 ASN 407 21.389 13.665 30.730 1.00 19.56 1DLC2959 ATOM 2836 ND2 ASN 407 21.969 11.955 32.047 1.00 24.80 1DLC2960 ATOM 2837 N LEU 408 19.283 15.447 31.692 1.00 25.59 1DLC2961 ATOM 2838 CA LEU 408 17.852 15.673 31.604 1.00 27.24 1DLC2962 ATOM 2839 C LEU 408 17.090 14.488 31.024 1.00 27.97 1DLC2963 ATOM 2840 O LEU 408 17.607 13.731 30.205 1.00 29.46 1DLC2964 ATOM 2841 CB LEU 408 17.561 16.945 30.790 1.00 28.54 1DLC2965 ATOM 2842 CG LEU 408 17.883 17.006 29.289 1.00 28.16 1DLC2966 ATOM 2843 CD1 LEU 408 16.710 16.462 28.507 1.00 31.12 1DLC2967 ATOM 2844 CD2 LEU 408 18.137 18.439 28.859 1.00 25.06 1DLC2968 ATOM 2845 N ALA 409 15.863 14.319 31.489 1.00 27.95 1DLC2969 ATOM 2846 CA ALA 409 14.990 13.263 31.011 1.00 26.71 1DLC2970 ATOM 2847 C ALA 409 13.750 13.974 30.501 1.00 26.39 1DLC2971 ATOM 2848 O ALA 409 13.185 14.819 31.197 1.00 27.94 1DLC2972 ATOM 2849 CB ALA 409 14.628 12.317 32.145 1.00 25.33 1DLC2973 ATOM 2850 N VAL 410 13.376 13.701 29.259 1.00 26.74 1DLC2974 ATOM 2851 CA VAL 410 12.189 14.312 28.670 1.00 27.20 1DLC2975 ATOM 2852 C VAL 410 10.956 13.404 28.802 1.00 28.76 1DLC2976 ATOM 2853 O VAL 410 10.885 12.345 28.179 1.00 31.07 1DLC2977 ATOM 2854 CB VAL 410 12.419 14.650 27.183 1.00 27.70 1DLC2978 ATOM 2855 CG1 VAL 410 11.162 15.238 26.567 1.00 25.34 1DLC2979 ATOM 2856 CG2 VAL 410 13.561 15.627 27.050 1.00 28.45 1DLC2980 ATOM 2857 N TRP 411 10.027 13.792 29.669 1.00 28.92 1DLC2981 ATOM 2858 CA TRP 411 8.787 13.047 29.871 1.00 32.40 1DLC2982 ATOM 2859 C TRP 411 7.681 13.644 28.982 1.00 36.76 1DLC2983 ATOM 2860 O TRP 411 7.783 14.797 28.558 1.00 37.48 1DLC2984 ATOM 2861 CB TRP 411 8.374 13.087 31.341 1.00 30.13 1DLC2985 ATOM 2862 CG TRP 411 9.146 12.153 32.224 1.00 31.99 1DLC2986 ATOM 2863 CD1 TRP 411 10.500 12.010 32.283 1.00 32.36 1DLC2987 ATOM 2864 CD2 TRP 411 8.609 11.291 33.237 1.00 33.30 1DLC2988 ATOM 2865 NE1 TRP 411 10.841 11.127 33.274 1.00 31.66 1DLC2989 ATOM 2866 CE2 TRP 411 9.700 10.671 33.878 1.00 34.52 1DLC2990 ATOM 2867 CE3 TRP 411 7.310 10.988 33.670 1.00 33.48 1DLC2991 ATOM 2868 CZ2 TRP 411 9.534 9.767 34.938 1.00 37.09 1DLC2992 ATOM 2869 CZ3 TRP 411 7.146 10.089 34.725 1.00 33.78 1DLC2993 ATOM 2870 CH2 TRP 411 8.253 9.492 35.345 1.00 33.59 1DLC2994 ATOM 2871 N PRO 412 6.574 12.900 28.755 1.00 41.54 1DLC2995 ATOM 2872 CA PRO 412 5.451 13.348 27.917 1.00 41.87 1DLC2996 ATOM 2873 C PRO 412 4.993 14.776 28.158 1.00 43.64 1DLC2997 ATOM 2874 O PRO 412 4.725 15.517 27.218 1.00 46.92 1DLC2998 ATOM 2875 CB PRO 412 4.349 12.361 28.277 1.00 39.76 1DLC2999 ATOM 2876 CG PRO 412 5.098 11.130 28.537 1.00 42.46 1DLC3000 ATOM 2877 CD PRO 412 6.231 11.620 29.399 1.00 41.84 1DLC3001 ATOM 2878 N SER 413 4.901 15.157 29.421 1.00 45.10 1DLC3002 ATOM 2879 CA SER 413 4.460 16.501 29.764 1.00 49.60 1DLC3003 ATOM 2880 C SER 413 5.322 17.110 30.873 1.00 49.62 1DLC3004 ATOM 2881 O SER 413 4.843 17.900 31.695 1.00 51.51 1DLC3005 ATOM 2882 CB SER 413 2.998 16.446 30.199 1.00 51.77 1DLC3006 ATOM 2883 OG SER 413 2.797 15.328 31.045 1.00 57.37 1DLC3007 ATOM 2884 N ALA 414 6.607 16.764 30.865 1.00 45.33 1DLC3008 ATOM 2885 CA ALA 414 7.534 17.257 31.871 1.00 38.96 1DLC3009 ATOM 2886 C ALA 414 8.979 16.981 31.485 1.00 36.86 1DLC3010 ATOM 2887 O ALA 414 9.275 16.041 30.750 1.00 36.90 1DLC3011 ATOM 2888 CB ALA 414 7.227 16.613 33.222 1.00 36.07 1DLC3012 ATOM 2889 N VAL 415 9.874 17.834 31.959 1.00 31.55 1DLC3013 ATOM 2890 CA VAL 415 11.294 17.667 31.713 1.00 28.69 1DLC3014 ATOM 2891 C VAL 415 11.957 17.736 33.083 1.00 27.90 1DLC3015 ATOM 2892 O VAL 415 11.636 18.604 33.895 1.00 28.78 1DLC3016 ATOM 2893 CB VAL 415 11.850 18.764 30.770 1.00 26.51 1DLC3017 ATOM 2894 CG1 VAL 415 13.373 18.695 30.699 1.00 27.88 1DLC3018 ATOM 2895 CG2 VAL 415 11.272 18.594 29.379 1.00 24.80 1DLC3019 ATOM 2896 N TYR 416 12.806 16.760 33.372 1.00 25.67 1DLC3020 ATOM 2897 CA TYR 416 13.504 16.713 34.648 1.00 26.02 1DLC3021 ATOM 2898 C TYR 416 14.992 16.821 34.407 1.00 26.24 1DLC3022 ATOM 2899 O TYR 416 15.537 16.120 33.560 1.00 28.40 1DLC3023 ATOM 2900 CB TYR 416 13.209 15.399 35.366 1.00 26.73 1DLC3024 ATOM 2901 CG TYR 416 11.746 15.180 35.657 1.00 29.24 1DLC3025 ATOM 2902 CD1 TYR 416 10.910 14.571 34.720 1.00 30.70 1DLC3026 ATOM 2903 CD2 TYR 416 11.194 15.583 36.869 1.00 28.65 1DLC3027 ATOM 2904 CE1 TYR 416 9.567 14.373 34.985 1.00 30.31 1DLC3028 ATOM 2905 CE2 TYR 416 9.857 15.387 37.144 1.00 31.22 1DLC3029 ATOM 2906 CZ TYR 416 9.049 14.784 36.200 1.00 32.49 1DLC3030 ATOM 2907 OH TYR 416 7.716 14.603 36.473 1.00 38.69 1DLC3031 ATOM 2908 N SER 417 15.650 17.706 35.138 1.00 27.76 1DLC3032 ATOM 2909 CA SER 417 17.090 17.883 34.986 1.00 28.62 1DLC3033 ATOM 2910 C SER 417 17.796 18.114 36.319 1.00 28.34 1DLC3034 ATOM 2911 O SER 417 17.236 18.706 37.242 1.00 27.52 1DLC3035 ATOM 2912 CB SER 417 17.403 19.015 34.003 1.00 26.82 1DLC3036 ATOM 2913 OG SER 417 16.714 20.196 34.351 1.00 31.53 1DLC3037 ATOM 2914 N GLY 418 19.016 17.602 36.430 1.00 28.56 1DLC3038 ATOM 2915 CA GLY 418 19.766 17.766 37.660 1.00 27.48 1DLC3039 ATOM 2916 C GLY 418 21.269 17.710 37.478 1.00 27.67 1DLC3040 ATOM 2917 O GLY 418 21.769 17.358 36.397 1.00 26.87 1DLC3041 ATOM 2918 N VAL 419 21.984 18.098 38.532 1.00 27.26 1DLC3042 ATOM 2919 CA VAL 419 23.446 18.087 38.551 1.00 23.88 1DLC3043 ATOM 2920 C VAL 419 23.883 16.673 38.946 1.00 24.66 1DLC3044 ATOM 2921 O VAL 419 23.612 16.192 40.047 1.00 23.69 1DLC3045 ATOM 2922 CB VAL 419 23.992 19.146 39.531 1.00 22.05 1DLC3046 ATOM 2923 CG1 VAL 419 25.513 19.176 39.498 1.00 20.25 1DLC3047 ATOM 2924 CG2 VAL 419 23.424 20.511 39.171 1.00 19.09 1DLC3048 ATOM 2925 N THR 420 24.552 16.006 38.022 1.00 24.57 1DLC3049 ATOM 2926 CA THR 420 24.965 14.628 38.227 1.00 26.41 1DLC3050 ATOM 2927 C THR 420 26.407 14.410 38.671 1.00 29.16 1DLC3051 ATOM 2928 O THR 420 26.720 13.410 39.323 1.00 30.90 1DLC3052 ATOM 2929 CB THR 420 24.781 13.874 36.938 1.00 26.62 1DLC3053 ATOM 2930 OG1 THR 420 25.586 14.506 35.944 1.00 28.39 1DLC3054 ATOM 2931 CG2 THR 420 23.329 13.938 36.484 1.00 27.96 1DLC3055 ATOM 2932 N LYS 421 27.292 15.325 38.295 1.00 31.11 1DLC3056 ATOM 2933 CA LYS 421 28.704 15.194 38.646 1.00 30.22 1DLC3057 ATOM 2934 C LYS 421 29.363 16.550 38.868 1.00 28.76 1DLC3058 ATOM 2935 O LYS 421 29.099 17.506 38.138 1.00 26.51 1DLC3059 ATOM 2936 CB LYS 421 29.433 14.443 37.526 1.00 29.98 1DLC3060 ATOM 2937 CG LYS 421 30.858 14.012 37.820 1.00 29.15 1DLC3061 ATOM 2938 CD LYS 421 31.539 13.708 36.499 1.00 33.33 1DLC3062 ATOM 2939 CE LYS 421 33.002 13.320 36.640 1.00 36.06 1DLC3063 ATOM 2940 NZ LYS 421 33.195 11.871 36.934 1.00 44.02 1DLC3064 ATOM 2941 N VAL 422 30.191 16.637 39.904 1.00 28.39 1DLC3065 ATOM 2942 CA VAL 422 30.912 17.872 40.208 1.00 28.83 1DLC3066 ATOM 2943 C VAL 422 32.374 17.589 40.571 1.00 28.74 1DLC3067 ATOM 2944 O VAL 422 32.679 16.920 41.562 1.00 24.14 1DLC3068 ATOM 2945 CB VAL 422 30.269 18.688 41.364 1.00 28.45 1DLC3069 ATOM 2946 CG1 VAL 422 30.903 20.084 41.428 1.00 26.59 1DLC3070 ATOM 2947 CG2 VAL 422 28.760 18.792 41.187 1.00 26.33 1DLC3071 ATOM 2948 N GLU 423 33.277 18.111 39.756 1.00 30.40 1DLC3072 ATOM 2949 CA GLU 423 34.697 17.934 39.988 1.00 32.36 1DLC3073 ATOM 2950 C GLU 423 35.337 19.193 40.577 1.00 30.72 1DLC3074 ATOM 2951 O GLU 423 35.353 20.255 39.952 1.00 29.33 1DLC3075 ATOM 2952 CB GLU 423 35.385 17.560 38.684 1.00 35.60 1DLC3076 ATOM 2953 CG GLU 423 36.857 17.283 38.819 1.00 46.42 1DLC3077 ATOM 2954 CD GLU 423 37.401 16.588 37.596 1.00 54.46 1DLC3078 ATOM 2955 OE1 GLU 423 37.241 15.348 37.502 1.00 59.71 1DLC3079 ATOM 2956 OE2 GLU 423 37.964 17.283 36.720 1.00 58.05 1DLC3080 ATOM 2957 N PHE 424 35.833 19.066 41.797 1.00 28.13 1DLC3081 ATOM 2958 CA PHE 424 36.491 20.167 42.486 1.00 29.49 1DLC3082 ATOM 2959 C PHE 424 38.029 20.130 42.355 1.00 30.85 1DLC3083 ATOM 2960 O PHE 424 38.672 19.105 42.628 1.00 30.79 1DLC3084 ATOM 2961 CB PHE 424 36.134 20.139 43.975 1.00 29.46 1DLC3085 ATOM 2962 CG PHE 424 34.662 20.205 44.253 1.00 30.25 1DLC3086 ATOM 2963 CD1 PHE 424 34.019 21.434 44.378 1.00 29.50 1DLC3087 ATOM 2964 CD2 PHE 424 33.923 19.043 44.422 1.00 29.43 1DLC3088 ATOM 2965 CE1 PHE 424 32.668 21.504 44.670 1.00 27.70 1DLC3089 ATOM 2966 CE2 PHE 424 32.572 19.100 44.714 1.00 29.35 1DLC3090 ATOM 2967 CZ PHE 424 31.942 20.336 44.840 1.00 30.09 1DLC3091 ATOM 2968 N SER 425 38.613 21.249 41.937 1.00 29.43 1DLC3092 ATOM 2969 CA SER 425 40.065 21.361 41.830 1.00 25.64 1DLC3093 ATOM 2970 C SER 425 40.569 22.074 43.080 1.00 27.43 1DLC3094 ATOM 2971 O SER 425 40.136 23.184 43.390 1.00 27.70 1DLC3095 ATOM 2972 CB SER 425 40.469 22.167 40.603 1.00 24.73 1DLC3096 ATOM 2973 OG SER 425 40.202 21.458 39.410 1.00 27.45 1DLC3097 ATOM 2974 N GLN 426 41.459 21.428 43.815 1.00 29.40 1DLC3098 ATOM 2975 CA GLN 426 42.010 22.018 45.028 1.00 34.28 1DLC3099 ATOM 2976 C GLN 426 43.541 22.162 45.029 1.00 37.43 1DLC3100 ATOM 2977 O GLN 426 44.257 21.428 44.344 1.00 38.20 1DLC3101 ATOM 2978 CB GLN 426 41.548 21.225 46.251 1.00 32.26 1DLC3102 ATOM 2979 CG GLN 426 41.830 19.736 46.179 1.00 33.97 1DLC3103 ATOM 2980 CD GLN 426 41.196 18.983 47.329 1.00 37.54 1DLC3104 ATOM 2981 OE1 GLN 426 40.063 19.258 47.714 1.00 39.93 1DLC3105 ATOM 2982 NE2 GLN 426 41.919 18.028 47.884 1.00 37.39 1DLC3106 ATOM 2983 N TYR 427 44.026 23.163 45.754 1.00 40.45 1DLC3107 ATOM 2984 CA TYR 427 45.455 23.402 45.872 1.00 41.55 1DLC3108 ATOM 2985 C TYR 427 45.819 23.459 47.351 1.00 42.39 1DLC3109 ATOM 2986 O TYR 427 45.118 24.072 48.149 1.00 40.82 1DLC3110 ATOM 2987 CB TYR 427 45.846 24.713 45.186 1.00 44.27 1DLC3111 ATOM 2988 CG TYR 427 47.328 25.006 45.252 1.00 49.58 1DLC3112 ATOM 2989 CD1 TYR 427 48.219 24.383 44.377 1.00 51.96 1DLC3113 ATOM 2990 CD2 TYR 427 47.848 25.883 46.209 1.00 49.78 1DLC3114 ATOM 2991 CE1 TYR 427 49.589 24.622 44.448 1.00 52.52 1DLC3115 ATOM 2992 CE2 TYR 427 49.218 26.128 46.292 1.00 52.70 1DLC3116 ATOM 2993 CZ TYR 427 50.083 25.493 45.408 1.00 53.61 1DLC3117 ATOM 2994 OH TYR 427 51.440 25.726 45.482 1.00 54.14 1DLC3118 ATOM 2995 N ASN 428 46.883 22.761 47.721 1.00 47.81 1DLC3119 ATOM 2996 CA ASN 428 47.350 22.743 49.104 1.00 51.08 1DLC3120 ATOM 2997 C ASN 428 48.569 23.666 49.205 1.00 54.49 1DLC3121 ATOM 2998 O ASN 428 49.669 23.296 48.790 1.00 55.38 1DLC3122 ATOM 2999 CB ASN 428 47.724 21.313 49.504 1.00 49.62 1DLC3123 ATOM 3000 CG ASN 428 48.045 21.180 50.977 1.00 49.60 1DLC3124 ATOM 3001 OD1 ASN 428 48.565 22.103 51.600 1.00 50.02 1DLC3125 ATOM 3002 ND2 ASN 428 47.762 20.021 51.536 1.00 51.27 1DLC3126 ATOM 3003 N ASP 429 48.365 24.871 49.732 1.00 57.69 1DLC3127 ATOM 3004 CA ASP 429 49.447 25.851 49.868 1.00 61.09 1DLC3128 ATOM 3005 C ASP 429 50.553 25.433 50.846 1.00 61.35 1DLC3129 ATOM 3006 O ASP 429 51.663 25.955 50.798 1.00 60.38 1DLC3130 ATOM 3007 CB ASP 429 48.884 27.234 50.231 1.00 63.50 1DLC3131 ATOM 3008 CG ASP 429 48.083 27.225 51.521 1.00 69.23 1DLC3132 ATOM 3009 OD1 ASP 429 47.071 26.486 51.596 1.00 74.87 1DLC3133 ATOM 3010 OD2 ASP 429 48.462 27.960 52.463 1.00 69.36 1DLC3134 ATOM 3011 N GLN 430 50.246 24.488 51.729 1.00 63.12 1DLC3135 ATOM 3012 CA GLN 430 51.227 23.987 52.688 1.00 64.06 1DLC3136 ATOM 3013 C GLN 430 52.185 23.064 51.938 1.00 60.99 1DLC3137 ATOM 3014 O GLN 430 53.368 23.353 51.802 1.00 62.46 1DLC3138 ATOM 3015 CB GLN 430 50.543 23.202 53.817 1.00 68.60 1DLC3139 ATOM 3016 CG GLN 430 49.735 24.035 54.821 1.00 77.24 1DLC3140 ATOM 3017 CD GLN 430 48.372 24.495 54.295 1.00 83.08 1DLC3141 ATOM 3018 OE1 GLN 430 48.121 25.694 54.164 1.00 86.17 1DLC3142 ATOM 3019 NE2 GLN 430 47.483 23.546 54.020 1.00 82.81 1DLC3143 ATOM 3020 N THR 431 51.643 21.973 51.409 1.00 57.70 1DLC3144 ATOM 3021 CA THR 431 52.425 20.992 50.658 1.00 54.67 1DLC3145 ATOM 3022 C THR 431 52.553 21.360 49.179 1.00 53.42 1DLC3146 ATOM 3023 O THR 431 52.775 20.505 48.334 1.00 52.29 1DLC3147 ATOM 3024 CB THR 431 51.786 19.594 50.760 1.00 54.43 1DLC3148 ATOM 3025 OG1 THR 431 50.488 19.617 50.155 1.00 55.57 1DLC3149 ATOM 3026 CG2 THR 431 51.627 19.188 52.223 1.00 54.20 1DLC3150 ATOM 3027 N ASP 432 52.399 22.643 48.883 1.00 55.66 1DLC3151 ATOM 3028 CA ASP 432 52.476 23.176 47.526 1.00 59.05 1DLC3152 ATOM 3029 C ASP 432 52.136 22.273 46.343 1.00 59.61 1DLC3153 ATOM 3030 O ASP 432 52.945 22.109 45.428 1.00 61.57 1DLC3154 ATOM 3031 CB ASP 432 53.816 23.875 47.288 1.00 63.68 1DLC3155 ATOM 3032 CG ASP 432 53.877 25.252 47.934 1.00 69.48 1DLC3156 ATOM 3033 OD1 ASP 432 53.439 26.238 47.293 1.00 70.82 1DLC3157 ATOM 3034 OD2 ASP 432 54.360 25.347 49.086 1.00 71.66 1DLC3158 ATOM 3035 N GLU 433 50.928 21.711 46.346 1.00 59.44 1DLC3159 ATOM 3036 CA GLU 433 50.480 20.871 45.233 1.00 57.29 1DLC3160 ATOM 3037 C GLU 433 48.957 20.787 45.047 1.00 52.84 1DLC3161 ATOM 3038 O GLU 433 48.178 20.915 45.994 1.00 46.51 1DLC3162 ATOM 3039 CB GLU 433 51.137 19.476 45.260 1.00 63.46 1DLC3163 ATOM 3040 CG GLU 433 50.290 18.331 45.795 1.00 69.79 1DLC3164 ATOM 3041 CD GLU 433 50.272 18.275 47.305 1.00 74.20 1DLC3165 ATOM 3042 OE1 GLU 433 51.179 17.634 47.887 1.00 75.74 1DLC3166 ATOM 3043 OE2 GLU 433 49.349 18.868 47.907 1.00 78.38 1DLC3167 ATOM 3044 N ALA 434 48.553 20.634 43.792 1.00 51.12 1DLC3168 ATOM 3045 CA ALA 434 47.146 20.552 43.419 1.00 50.02 1DLC3169 ATOM 3046 C ALA 434 46.636 19.113 43.301 1.00 48.51 1DLC3170 ATOM 3047 O ALA 434 47.418 18.168 43.249 1.00 51.46 1DLC3171 ATOM 3048 CB ALA 434 46.913 21.302 42.107 1.00 49.76 1DLC3172 ATOM 3049 N SER 435 45.316 18.969 43.250 1.00 44.96 1DLC3173 ATOM 3050 CA SER 435 44.650 17.674 43.139 1.00 38.99 1DLC3174 ATOM 3051 C SER 435 43.159 17.914 42.940 1.00 39.56 1DLC3175 ATOM 3052 O SER 435 42.693 19.048 42.999 1.00 38.70 1DLC3176 ATOM 3053 CB SER 435 44.845 16.857 44.415 1.00 35.36 1DLC3177 ATOM 3054 OG SER 435 44.241 17.492 45.528 1.00 32.98 1DLC3178 ATOM 3055 N THR 436 42.407 16.847 42.705 1.00 38.68 1DLC3179 ATOM 3056 CA THR 436 40.967 16.979 42.526 1.00 36.86 1DLC3180 ATOM 3057 C THR 436 40.171 16.007 43.392 1.00 36.34 1DLC3181 ATOM 3058 O THR 436 40.679 14.970 43.823 1.00 37.73 1DLC3182 ATOM 3059 CB THR 436 40.540 16.757 41.065 1.00 35.68 1DLC3183 ATOM 3060 OG1 THR 436 40.788 15.397 40.699 1.00 41.63 1DLC3184 ATOM 3061 CG2 THR 436 41.313 17.674 40.130 1.00 37.09 1DLC3185 ATOM 3062 N GLN 437 38.947 16.407 43.713 1.00 35.55 1DLC3186 ATOM 3063 CA GLN 437 38.009 15.597 44.485 1.00 33.02 1DLC3187 ATOM 3064 C GLN 437 36.709 15.729 43.723 1.00 34.09 1DLC3188 ATOM 3065 O GLN 437 36.391 16.809 43.227 1.00 34.18 1DLC3189 ATOM 3066 CB GLN 437 37.813 16.140 45.894 1.00 30.43 1DLC3190 ATOM 3067 CG GLN 437 38.812 15.635 46.887 1.00 30.16 1DLC3191 ATOM 3068 CD GLN 437 38.380 15.896 48.305 1.00 32.30 1DLC3192 ATOM 3069 OE1 GLN 437 37.962 14.984 49.015 1.00 36.80 1DLC3193 ATOM 3070 NE2 GLN 437 38.458 17.144 48.726 1.00 34.86 1DLC3194 ATOM 3071 N THR 438 35.966 14.644 43.575 1.00 34.88 1DLC3195 ATOM 3072 CA THR 438 34.725 14.759 42.828 1.00 35.70 1DLC3196 ATOM 3073 C THR 438 33.533 14.042 43.417 1.00 34.07 1DLC3197 ATOM 3074 O THR 438 33.663 13.090 44.177 1.00 35.71 1DLC3198 ATOM 3075 CB THR 438 34.857 14.280 41.346 1.00 37.66 1DLC3199 ATOM 3076 OG1 THR 438 34.466 12.905 41.251 1.00 37.09 1DLC3200 ATOM 3077 CG2 THR 438 36.286 14.453 40.812 1.00 32.87 1DLC3201 ATOM 3078 N TYR 439 32.366 14.560 43.074 1.00 34.88 1DLC3202 ATOM 3079 CA TYR 439 31.100 13.988 43.473 1.00 32.18 1DLC3203 ATOM 3080 C TYR 439 30.575 13.313 42.197 1.00 32.47 1DLC3204 ATOM 3081 O TYR 439 30.636 13.888 41.102 1.00 30.88 1DLC3205 ATOM 3082 CB TYR 439 30.141 15.089 43.936 1.00 29.14 1DLC3206 ATOM 3083 CG TYR 439 28.691 14.683 43.824 1.00 30.66 1DLC3207 ATOM 3084 CD1 TYR 439 28.126 13.796 44.738 1.00 28.98 1DLC3208 ATOM 3085 CD2 TYR 439 27.902 15.117 42.751 1.00 27.98 1DLC3209 ATOM 3086 CE1 TYR 439 26.825 13.344 44.588 1.00 29.00 1DLC3210 ATOM 3087 CE2 TYR 439 26.598 14.667 42.595 1.00 26.79 1DLC3211 ATOM 3088 CZ TYR 439 26.072 13.778 43.518 1.00 25.85 1DLC3212 ATOM 3089 OH TYR 439 24.798 13.305 43.369 1.00 25.37 1DLC3213 ATOM 3090 N ASP 440 30.098 12.082 42.323 1.00 33.95 1DLC3214 ATOM 3091 CA ASP 440 29.568 11.366 41.162 1.00 36.24 1DLC3215 ATOM 3092 C ASP 440 28.231 10.735 41.551 1.00 37.15 1DLC3216 ATOM 3093 O ASP 440 28.152 10.014 42.547 1.00 37.73 1DLC3217 ATOM 3094 CB ASP 440 30.560 10.285 40.711 1.00 37.85 1DLC3218 ATOM 3095 CG ASP 440 30.332 9.831 39.277 1.00 40.56 1DLC3219 ATOM 3096 OD1 ASP 440 29.253 9.284 38.975 1.00 45.14 1DLC3220 ATOM 3097 OD2 ASP 440 31.246 10.006 38.442 1.00 44.83 1DLC3221 ATOM 3098 N SER 441 27.177 11.035 40.794 1.00 36.81 1DLC3222 ATOM 3099 CA SER 441 25.851 10.483 41.087 1.00 36.80 1DLC3223 ATOM 3100 C SER 441 25.825 8.972 40.882 1.00 39.60 1DLC3224 ATOM 3101 O SER 441 25.000 8.271 41.467 1.00 40.38 1DLC3225 ATOM 3102 CB SER 441 24.781 11.133 40.212 1.00 33.16 1DLC3226 ATOM 3103 OG SER 441 24.910 10.741 38.857 1.00 34.23 1DLC3227 ATOM 3104 N LYS 442 26.738 8.495 40.039 1.00 41.35 1DLC3228 ATOM 3105 CA LYS 442 26.901 7.078 39.701 1.00 45.48 1DLC3229 ATOM 3106 C LYS 442 25.977 6.509 38.618 1.00 46.07 1DLC3230 ATOM 3107 O LYS 442 26.260 5.446 38.055 1.00 49.36 1DLC3231 ATOM 3108 CB LYS 442 26.905 6.192 40.953 1.00 49.45 1DLC3232 ATOM 3109 CG LYS 442 28.279 5.606 41.309 1.00 56.04 1DLC3233 ATOM 3110 CD LYS 442 28.626 4.379 40.446 1.00 58.91 1DLC3234 ATOM 3111 CE LYS 442 29.111 4.762 39.050 1.00 60.19 1DLC3235 ATOM 3112 NZ LYS 442 28.866 3.683 38.044 1.00 60.75 1DLC3236 ATOM 3113 N ARG 443 24.885 7.201 38.310 1.00 43.51 1 1DLC3237 ATOM 3114 CA ARG 443 24.001 6.738 37.247 1.00 40.12 1 1DLC3238 ATOM 3115 C ARG 443 23.716 7.807 36.191 1.00 39.29 1 1DLC3239 ATOM 3116 O ARG 443 23.231 8.897 36.498 1.00 39.09 1 1DLC3240 ATOM 3117 CB AARG 443 22.686 6.168 37.792 0.50 39.58 1 1DLC3241 ATOM 3118 CB BARG 443 22.701 6.194 37.849 0.50 39.12 1 1DLC3242 ATOM 3119 CG AARG 443 21.828 5.580 36.678 0.50 38.20 1 1DLC3243 ATOM 3120 CG BARG 443 21.551 6.015 36.868 0.50 37.50 1 1DLC3244 ATOM 3121 CD AARG 443 20.703 4.678 37.156 0.50 38.35 1 1DLC3245 ATOM 3122 CD BARG 443 20.501 5.057 37.413 0.50 36.41 1 1DLC3246 ATOM 3123 NE AARG 443 20.266 3.824 36.050 0.50 38.24 1 1DLC3247 ATOM 3124 NE BARG 443 20.317 5.184 38.857 0.50 34.60 1 1DLC3248 ATOM 3125 CZ AARG 443 19.076 3.238 35.951 0.50 37.74 1 1DLC3249 ATOM 3126 CZ BARG 443 19.823 4.226 39.636 0.50 34.26 1 1DLC3250 ATOM 3127 NH1 AARG 443 18.160 3.392 36.895 0.50 38.52 1 1DLC3251 ATOM 3128 NH1 BARG 443 19.452 3.064 39.110 0.50 31.83 1 1DLC3252 ATOM 3129 NH2 AARG 443 18.798 2.508 34.882 0.50 37.87 1 1DLC3253 ATOM 3136 NH2 BARG 443 19.727 4.418 40.948 0.50 31.14 1 1DLC3254 ATOM 3131 N ASN 444 24.070 7.481 34.950 1.00 40.97 1DLC3255 ATOM 3132 CA ASN 444 23.882 8.350 33.784 1.00 41.75 1DLC3256 ATOM 3133 C ASN 444 24.271 9.814 34.045 1.00 42.79 1DLC3257 ATOM 3134 O ASN 444 23.421 10.700 34.174 1.00 42.71 1DLC3258 ATOM 3135 CB ASN 444 22.446 8.230 33.271 1.00 43.21 1DLC3259 ATOM 3136 CG ASN 444 22.280 8.764 31.862 1.00 44.75 1DLC3260 ATOM 3137 OD1 ASN 444 23.258 9.086 31.182 1.00 47.47 1DLC3261 ATOM 3138 ND2 ASN 444 21.040 8.867 31.418 1.00 45.66 1DLC3262 ATOM 3139 N VAL 445 25.579 10.041 34.079 1.00 42.96 1DLC3263 ATOM 3140 CA VAL 445 26.195 11.345 34.342 1.00 41.13 1DLC3264 ATOM 3141 C VAL 445 26.035 12.460 33.282 1.00 39.24 1DLC3265 ATOM 3142 O VAL 445 26.037 13.641 33.602 1.00 41.51 1DLC3266 ATOM 3143 CB VAL 445 27.694 11.117 34.702 1.00 41.94 1DLC3267 ATOM 3144 CG1 VAL 445 28.516 12.385 34.554 1.00 43.22 1DLC3268 ATOM 3145 CG2 VAL 445 27.796 10.562 36.116 1.00 37.86 1DLC3269 ATOM 3146 N GLY 446 25.888 12.108 32.020 1.00 38.45 1DLC3270 ATOM 3147 CA GLY 446 25.737 13.157 31.032 1.00 37.87 1DLC3271 ATOM 3148 C GLY 446 27.023 13.933 30.806 1.00 38.06 1DLC3272 ATOM 3149 O GLY 446 28.108 13.458 31.137 1.00 39.17 1DLC3273 ATOM 3150 N ALA 447 26.899 15.146 30.276 1.00 38.09 1DLC3274 ATOM 3151 CA ALA 447 28.060 15.980 29.973 1.00 37.35 1DLC3275 ATOM 3152 C ALA 447 28.222 17.226 30.847 1.00 35.81 1DLC3276 ATOM 3153 O ALA 447 27.291 17.651 31.535 1.00 35.86 1DLC3277 ATOM 3154 CB ALA 447 28.043 16.373 28.490 1.00 38.30 1DLC3278 ATOM 3155 N VAL 448 29.426 17.794 30.818 1.00 33.69 1DLC3279 ATOM 3156 CA VAL 448 29.736 18.992 31.590 1.00 32.06 1DLC3280 ATOM 3157 C VAL 448 29.041 20.194 30.976 1.00 30.84 1DLC3281 ATOM 3158 O VAL 448 29.117 20.413 29.771 1.00 30.03 1DLC3282 ATOM 3159 CB VAL 448 31.275 19.263 31.695 1.00 30.42 1DLC3283 ATOM 3160 CG1 VAL 448 31.936 18.203 32.547 1.00 30.39 1DLC3284 ATOM 3161 CG2 VAL 448 31.919 19.283 30.334 1.00 28.17 1DLC3285 ATOM 3162 N SER 449 28.324 20.942 31.805 1.00 29.95 1DLC3286 ATOM 3163 CA SER 449 27.609 22.116 31.326 1.00 30.08 1DLC3287 ATOM 3164 C SER 449 27.940 23.393 32.100 1.00 29.27 1DLC3288 ATOM 3165 O SER 449 27.571 24.486 31.675 1.00 29.45 1DLC3289 ATOM 3166 CB SER 449 26.093 21.875 31.386 1.00 31.17 1DLC3290 ATOM 3167 OG SER 449 25.616 21.864 32.723 1.00 32.27 1DLC3291 ATOM 3168 N TRP 450 28.668 23.264 33.206 1.00 26.45 1DLC3292 ATOM 3169 CA TRP 450 28.993 24.427 34.023 1.00 24.97 1DLC3293 ATOM 3170 C TRP 450 30.444 24.442 34.525 1.00 25.78 1DLC3294 ATOM 3171 O TRP 450 30.903 23.514 35.193 1.00 26.98 1DLC3295 ATOM 3172 CB TRP 450 28.003 24.475 35.198 1.00 22.55 1DLC3296 ATOM 3173 CG TRP 450 28.003 25.718 36.062 1.00 24.05 1DLC3297 ATOM 3174 CD1 TRP 450 27.071 26.723 36.046 1.00 24.31 1DLC3298 ATOM 3175 CD2 TRP 450 28.864 25.994 37.181 1.00 22.36 1DLC3299 ATOM 3176 NE1 TRP 450 27.282 27.585 37.101 1.00 24.38 1DLC3300 ATOM 3177 CE2 TRP 450 28.376 27.163 37.809 1.00 22.02 1DLC3301 ATOM 3178 CE3 TRP 450 29.989 25.361 37.719 1.00 23.01 1DLC3302 ATOM 3179 CZ2 TRP 450 28.970 27.705 38.946 1.00 23.92 1DLC3303 ATOM 3180 CZ3 TRP 450 30.579 25.902 38.852 1.00 23.85 1DLC3304 ATOM 3181 CH2 TRP 450 30.068 27.062 39.451 1.00 24.68 1DLC3305 ATOM 3182 N ASP 451 31.148 25.529 34.227 1.00 26.82 1DLC3306 ATOM 3183 CA ASP 451 32.541 25.703 34.640 1.00 23.64 1DLC3307 ATOM 3184 C ASP 451 32.701 27.046 35.359 1.00 22.66 1DLC3308 ATOM 3185 O ASP 451 32.479 28.103 34.760 1.00 20.61 1DLC3309 ATOM 3186 CB ASP 451 33.451 25.675 33.406 1.00 22.67 1DLC3310 ATOM 3187 CG ASP 451 34.920 25.461 33.749 1.00 24.25 1DLC3311 ATOM 3188 OD1 ASP 451 35.325 25.616 34.919 1.00 24.75 1DLC3312 ATOM 3189 OD2 ASP 451 35.674 25.116 32.824 1.00 24.52 1DLC3313 ATOM 3190 N SER 452 33.106 27.001 36.629 1.00 20.91 1DLC3314 ATOM 3191 CA SER 452 33.307 28.219 37.432 1.00 22.01 1DLC3315 ATOM 3192 C SER 452 34.262 29.231 36.786 1.00 23.43 1DLC3316 ATOM 3193 O SER 452 34.036 30.443 36.833 1.00 23.61 1DLC3317 ATOM 3194 CB SER 452 33.799 27.868 38.840 1.00 20.07 1DLC3318 ATOM 3195 OG SER 452 34.950 27.049 38.793 1.00 22.47 1DLC3319 ATOM 3196 N ILE 453 35.291 28.724 36.122 1.00 25.73 1DLC3320 ATOM 3197 CA ILE 453 36.272 29.571 35.454 1.00 27.62 1DLC3321 ATOM 3198 C ILE 453 35.641 30.563 34.469 1.00 25.55 1DLC3322 ATOM 3199 O ILE 453 36.181 31.645 34.255 1.00 28.13 1DLC3323 ATOM 3200 CB ILE 453 37.383 28.691 34.786 1.00 29.82 1DLC3324 ATOM 3201 CG1 ILE 453 38.345 28.183 35.866 1.00 35.65 1DLC3325 ATOM 3202 CG2 ILE 453 38.154 29.446 33.730 1.00 32.32 1DLC3326 ATOM 3203 CD1 ILE 453 38.910 29.287 36.786 1.00 36.52 1DLC3327 ATOM 3204 N ASP 454 34.474 30.225 33.926 1.00 22.83 1DLC3328 ATOM 3205 CA ASP 454 33.786 31.107 32.982 1.00 22.88 1DLC3329 ATOM 3206 C ASP 454 33.256 32.362 33.663 1.00 23.05 1DLC3330 ATOM 3207 O ASP 454 33.097 33.412 33.034 1.00 22.70 1DLC3331 ATOM 3208 CB ASP 454 32.598 30.397 32.337 1.00 29.00 1DLC3332 ATOM 3209 CG ASP 454 33.000 29.187 31.533 1.00 36.53 1DLC3333 ATOM 3210 OD1 ASP 454 33.975 29.279 30.749 1.00 38.64 1DLC3334 ATOM 3211 OD2 ASP 454 32.322 28.144 31.679 1.00 42.72 1DLC3335 ATOM 3212 N GLN 455 32.929 32.226 34.943 1.00 21.53 1DLC3336 ATOM 3213 CA GLN 455 32.388 33.330 35.711 1.00 19.71 1DLC3337 ATOM 3214 C GLN 455 33.440 33.991 36.574 1.00 21.92 1DLC3338 ATOM 3215 O GLN 455 33.399 35.198 36.801 1.00 26.53 1DLC3339 ATOM 3216 CB GLN 455 31.223 32.834 36.555 1.00 16.77 1DLC3340 ATOM 3217 CG GLN 455 30.108 32.308 35.690 1.00 22.31 1DLC3341 ATOM 3218 CD GLN 455 29.032 31.629 36.475 1.00 23.60 1DLC3342 ATOM 3219 OE1 GLN 455 28.575 32.150 37.468 1.00 24.05 1DLC3343 ATOM 3220 NE2 GLN 455 28.628 30.449 36.042 1.00 27.92 1DLC3344 ATOM 3221 N LEU 456 34.388 33.197 37.054 1.00 23.05 1DLC3345 ATOM 3222 CA LEU 456 35.469 33.709 37.894 1.00 22.56 1DLC3346 ATOM 3223 C LEU 456 36.813 33.349 37.274 1.00 20.68 1DLC3347 ATOM 3224 O LEU 456 37.508 32.440 37.730 1.00 19.98 1DLC3348 ATOM 3225 CB LEU 456 35.357 33.149 39.316 1.00 20.94 1DLC3349 ATOM 3226 CG LEU 456 34.034 33.435 40.044 1.00 22.46 1DLC3350 ATOM 3227 CD1 LEU 456 34.021 32.668 41.344 1.00 21.63 1DLC3351 ATOM 3228 CD2 LEU 456 33.850 34.935 40.297 1.00 17.51 1DLC3352 ATOM 3229 N PRO 457 37.193 34.071 36.211 1.00 21.65 1DLC3353 ATOM 3230 CA PRO 457 38.453 33.850 35.500 1.00 22.86 1DLC3354 ATOM 3231 C PRO 457 39.648 33.998 36.454 1.00 25.36 1DLC3355 ATOM 3232 O PRO 457 39.500 34.486 37.585 1.00 23.67 1DLC3356 ATOM 3233 CB PRO 457 38.450 34.975 34.458 1.00 21.76 1DLC3357 ATOM 3234 CG PRO 457 37.016 35.300 34.277 1.00 20.92 1DLC3358 ATOM 3235 CD PRO 457 36.495 35.251 35.673 1.00 19.85 1DLC3359 ATOM 3236 N PRO 458 40.843 33.557 36.022 1.00 25.47 1DLC3360 ATOM 3237 CA PRO 458 42.028 33.671 36.878 1.00 24.94 1DLC3361 ATOM 3238 C PRO 458 42.597 35.093 36.789 1.00 25.68 1DLC3362 ATOM 3239 O PRO 458 42.340 35.818 35.819 1.00 22.11 1DLC3363 ATOM 3240 CB PRO 458 43.008 32.672 36.251 1.00 24.27 1DLC3364 ATOM 3241 CG PRO 458 42.197 31.916 35.224 1.00 26.36 1DLC3365 ATOM 3242 CD PRO 458 41.187 32.894 34.759 1.00 23.11 1DLC3366 ATOM 3243 N GLU 459 43.343 35.504 37.809 1.00 26.71 1DLC3367 ATOM 3244 CA GLU 459 43.950 36.827 37.788 1.00 33.63 1DLC3368 ATOM 3245 C GLU 459 44.956 36.884 36.646 1.00 37.69 1DLC3369 ATOM 3246 O GLU 459 45.090 37.907 35.971 1.00 37.94 1DLC3370 ATOM 3247 CB GLU 459 44.654 37.129 39.106 1.00 34.45 1DLC3371 ATOM 3248 CG GLU 459 43.711 37.364 40.269 1.00 38.75 1DLC3372 ATOM 3249 CD GLU 459 44.438 37.530 41.590 1.00 40.23 1DLC3373 ATOM 3250 OE1 GLU 459 45.676 37.372 41.614 1.00 44.97 1DLC3374 ATOM 3251 OE2 GLU 459 43.772 37.811 42.610 1.00 41.43 1DLC3375 ATOM 3252 N THR 460 45.640 35.765 36.419 1.00 42.42 1DLC3376 ATOM 3253 CA THR 460 46.634 35.668 35.352 1.00 46.99 1DLC3377 ATOM 3254 C THR 460 46.516 34.423 34.495 1.00 48.85 1DLC3378 ATOM 3255 O THR 460 46.385 33.310 35.006 1.00 49.59 1DLC3379 ATOM 3256 CB THR 460 48.091 35.669 35.892 1.00 47.16 1DLC3380 ATOM 3257 OG1 THR 460 48.212 34.744 36.980 1.00 48.60 1DLC3381 ATOM 3258 CG2 THR 460 48.502 37.051 36.348 1.00 52.25 1DLC3382 ATOM 3259 N THR 461 46.583 34.625 33.185 1.00 52.04 1DLC3383 ATOM 3260 CA THR 461 46.555 33.524 32.231 1.00 55.43 1DLC3384 ATOM 3261 C THR 461 48.009 33.128 31.950 1.00 59.08 1DLC3385 ATOM 3262 O THR 461 48.290 32.305 31.077 1.00 62.04 1DLC3386 ATOM 3263 CB THR 461 45.898 33.942 30.914 1.00 55.22 1DLC3387 ATOM 3264 OG1 THR 461 46.513 35.143 30.440 1.00 57.54 1DLC3388 ATOM 3265 CG2 THR 461 44.419 34.183 31.113 1.00 54.73 1DLC3389 ATOM 3266 N ASP 462 48.929 33.768 32.668 1.00 61.13 1DLC3390 ATOM 3267 CA ASP 462 50.355 33.499 32.542 1.00 63.77 1DLC3391 ATOM 3268 C ASP 462 50.749 32.240 33.319 1.00 62.37 1DLC3392 ATOM 3269 O ASP 462 51.321 31.308 32.757 1.00 63.78 1DLC3393 ATOM 3270 CB ASP 462 51.162 34.700 33.054 1.00 70.21 1DLC3394 ATOM 3271 CG ASP 462 51.831 35.485 31.930 1.00 76.55 1DLC3395 ATOM 3272 OD1 ASP 462 51.191 35.686 30.871 1.00 79.02 1DLC3396 ATOM 3273 OD2 ASP 462 53.004 35.901 32.110 1.00 79.69 1DLC3397 ATOM 3274 N GLU 463 50.437 32.224 34.612 1.00 60.14 1DLC3398 ATOM 3275 CA GLU 463 50.752 31.090 35.483 1.00 58.33 1DLC3399 ATOM 3276 C GLU 463 49.703 29.968 35.441 1.00 55.57 1DLC3400 ATOM 3277 O GLU 463 48.610 30.140 34.890 1.00 57.13 1DLC3401 ATOM 3278 CB GLU 463 50.886 31.575 36.922 1.00 60.04 1DLC3402 ATOM 3279 CG GLU 463 51.932 32.639 37.123 1.00 69.89 1DLC3403 ATOM 3280 CD GLU 463 52.244 32.859 38.594 1.00 77.10 1DLC3404 ATOM 3281 OE1 GLU 463 51.402 33.458 39.308 1.00 79.81 1DLC3405 ATOM 3282 OE2 GLU 463 53.331 32.418 39.041 1.00 81.43 1DLC3406 ATOM 3283 N PRO 464 50.034 28.785 35.996 1.00 51.32 1DLC3407 ATOM 3284 CA PRO 464 49.045 27.702 35.982 1.00 47.85 1DLC3408 ATOM 3285 C PRO 464 47.898 28.044 36.955 1.00 44.75 1DLC3409 ATOM 3286 O PRO 464 48.124 28.725 37.963 1.00 41.10 1DLC3410 ATOM 3287 CB PRO 464 49.867 26.486 36.435 1.00 47.06 1DLC3411 ATOM 3288 CG PRO 464 50.929 27.087 37.300 1.00 46.21 1DLC3412 ATOM 3289 CD PRO 464 51.328 28.309 36.521 1.00 48.64 1DLC3413 ATOM 3290 N LEU 465 46.686 27.570 36.657 1.00 41.80 1DLC3414 ATOM 3291 CA LEU 465 45.497 27.853 37.475 1.00 37.33 1DLC3415 ATOM 3292 C LEU 465 45.658 27.777 38.992 1.00 35.76 1DLC3416 ATOM 3293 O LEU 465 45.174 28.655 39.707 1.00 34.89 1DLC3417 ATOM 3294 CB LEU 465 44.311 26.981 37.047 1.00 38.95 1DLC3418 ATOM 3295 CG LEU 465 43.043 27.695 36.542 1.00 40.98 1DLC3419 ATOM 3296 CD1 LEU 465 41.879 26.706 36.476 1.00 41.37 1DLC3420 ATOM 3297 CD2 LEU 465 42.673 28.853 37.448 1.00 38.54 1DLC3421 ATOM 3298 N GLU 466 46.341 26.749 39.489 1.00 31.43 1DLC3422 ATOM 3299 CA GLU 466 46.534 26.620 40.930 1.00 32.27 1DLC3423 ATOM 3300 C GLU 466 47.368 27.763 41.518 1.00 31.84 1DLC3424 ATOM 3301 O GLU 466 47.493 27.895 42.737 1.00 33.28 1DLC3425 ATOM 3302 CB GLU 466 47.144 25.263 41.300 1.00 35.86 1DLC3426 ATOM 3303 CG GLU 466 48.603 25.078 40.917 1.00 41.48 1DLC3427 ATOM 3304 CD GLU 466 48.789 24.358 39.595 1.00 43.01 1DLC3428 ATOM 3305 OE1 GLU 466 48.001 24.585 38.650 1.00 43.46 1DLC3429 ATOM 3306 OE2 GLU 466 49.737 23.552 39.506 1.00 49.70 1DLC3430 ATOM 3307 N LYS 467 47.959 28.568 40.643 1.00 30.87 1DLC3431 ATOM 3308 CA LYS 467 48.753 29.716 41.071 1.00 34.88 1DLC3432 ATOM 3309 C LYS 467 48.053 31.033 40.739 1.00 30.95 1DLC3433 ATOM 3310 O LYS 467 48.050 31.955 41.537 1.00 34.01 1DLC3434 ATOM 3311 CB LYS 467 50.126 29.727 40.395 1.00 41.82 1DLC3435 ATOM 3312 CG LYS 467 51.091 28.619 40.784 1.00 48.67 1DLC3436 ATOM 3313 CD LYS 467 52.383 28.821 39.991 1.00 59.85 1DLC3437 ATOM 3314 CE LYS 467 53.387 27.682 40.140 1.00 63.85 1DLC3438 ATOM 3315 NZ LYS 467 54.585 27.912 39.262 1.00 63.42 1DLC3439 ATOM 3316 N GLY 468 47.462 31.113 39.553 1.00 29.04 1DLC3440 ATOM 3317 CA GLY 468 46.806 32.342 39.136 1.00 28.69 1DLC3441 ATOM 3318 C GLY 468 45.319 32.552 39.384 1.00 27.26 1DLC3442 ATOM 3319 O GLY 468 44.794 33.614 39.036 1.00 26.73 1DLC3443 ATOM 3320 N GLY 468 44.640 31.570 39.977 1.00 23.94 1DLC3444 ATOM 3321 CA TYR 469 43.207 31.689 40.243 1.00 23.65 1DLC3445 ATOM 3322 C TYR 469 42.874 32.954 41.064 1.00 26.78 1DLC3446 ATOM 3323 O TYR 469 43.728 33.498 41.762 1.00 29.85 1DLC3447 ATOM 3324 CB TYR 469 42.687 30.427 40.931 1.00 18.50 1DLC3448 ATOM 3325 CG TYR 469 43.069 30.300 42.384 1.00 18.68 1DLC3449 ATOM 3326 CD1 TYR 469 44.253 29.668 42.771 1.00 18.59 1DLC3450 ATOM 3327 CD2 TYR 469 42.228 30.789 43.381 1.00 17.48 1DLC3451 ATOM 3328 CE1 TYR 469 44.581 29.526 44.119 1.00 18.20 1DLC3452 ATOM 3329 CE2 TYR 469 42.543 30.655 44.722 1.00 17.54 1DLC3453 ATOM 3330 CZ TYR 469 43.715 30.025 45.088 1.00 19.23 1DLC3454 ATOM 3331 OH TYR 469 43.999 29.900 46.427 1.00 24.58 1DLC3455 ATOM 3332 N SER 470 41.637 33.430 40.970 1.00 26.56 1DLC3456 ATOM 3333 CA SER 470 41.235 34.646 41.684 1.00 26.36 1DLC3457 ATOM 3334 C SER 470 40.278 34.460 42.861 1.00 25.81 1DLC3458 ATOM 3335 O SER 470 40.118 35.364 43.689 1.00 27.24 1DLC3459 ATOM 3336 CB SER 470 40.604 35.631 40.701 1.00 26.16 1DLC3460 ATOM 3337 OG SER 470 39.445 35.070 40.106 1.00 24.14 1DLC3461 ATOM 3338 N HIS 471 39.623 33.305 42.926 1.00 24.96 1DLC3462 ATOM 3339 CA HIS 471 38.656 33.025 43.986 1.00 22.21 1DLC3463 ATOM 3340 C HIS 471 38.652 31.573 44.426 1.00 20.34 1DLC3464 ATOM 3341 O HIS 471 39.004 30.685 43.666 1.00 20.23 1DLC3465 ATOM 3342 CB HIS 471 37.234 33.342 43.501 1.00 24.72 1DLC3466 ATOM 3343 CG HIS 471 36.951 34.800 43.306 1.00 24.47 1DLC3467 ATOM 3344 ND1 HIS 471 37.260 35.474 42.142 1.00 22.67 1DLC3468 ATOM 3345 CD2 HIS 471 36.328 35.699 44.106 1.00 22.96 1DLC3469 ATOM 3346 CE1 HIS 471 36.835 36.720 24.232 1.00 22.12 1DLC3470 ATOM 3347 NE2 HIS 471 36.265 36.881 43.415 1.00 21.11 1DLC3471 ATOM 3348 N GLN 472 38.180 31.334 45.638 1.00 19.76 1DLC3472 ATOM 3349 CA GLN 472 38.079 29.979 46.155 1.00 20.82 1DLC3473 ATOM 3350 C GLN 472 36.680 29.724 46.709 1.00 22.36 1DLC3474 ATOM 3351 O GLN 472 35.976 30.664 47.097 1.00 22.13 1DLC3475 ATOM 3352 CB GLN 472 39.120 29.740 47.230 1.00 22.23 1DLC3476 ATOM 3353 CG GLN 472 39.115 30.769 48.313 1.00 29.71 1DLC3477 ATOM 3354 CD GLN 472 40.248 30.552 49.280 1.00 40.11 1DLC3478 ATOM 3355 OE1 GLN 472 40.174 29.680 50.151 1.00 41.87 1DLC3479 ATOM 3356 NE2 GLN 472 41.326 31.317 49.116 1.00 44.52 1DLC3480 ATOM 3357 N LEU 473 36.277 28.455 46.731 1.00 23.05 1DLC3481 ATOM 3358 CA LEU 473 34.959 28.054 47.221 1.00 20.06 1DLC3482 ATOM 3359 C LEU 473 34.794 28.248 48.725 1.00 20.03 1DLC3483 ATOM 3360 O LEU 473 35.637 27.833 49.517 1.00 19.02 1DLC3484 ATOM 3361 CB LEU 473 34.678 26.587 46.876 1.00 21.51 1DLC3485 ATOM 3362 CG LEU 473 33.401 26.198 46.118 1.00 22.58 1DLC3486 ATOM 3363 CD1 LEU 473 33.188 24.714 46.270 1.00 20.29 1DLC3487 ATOM 3364 CD2 LEU 473 32.181 26.940 46.633 1.00 20.63 1DLC3488 ATOM 3365 N ASN 474 33.685 28.862 49.108 1.00 20.98 1DLC3489 ATOM 3366 CA ASN 474 33.394 29.103 50.508 1.00 22.93 1DLC3490 ATOM 3367 C ASN 474 32.087 28.434 50.936 1.00 22.97 1DLC3491 ATOM 3368 O ASN 474 31.975 27.922 52.056 1.00 23.74 1DLC3492 ATOM 3369 CB ASN 474 33.327 30.612 50.777 1.00 24.38 1DLC3493 ATOM 3370 CG ASN 474 33.068 30.941 52.247 1.00 29.78 1DLC3494 ATOM 3371 OD1 ASN 474 32.237 31.780 52.563 1.00 38.30 1DLC3495 ATOM 3372 ND2 ASN 474 33.789 30.298 53.140 1.00 29.37 1DLC3496 ATOM 3373 N TYR 475 31.119 28.383 50.028 1.00 21.61 1DLC3497 ATOM 3374 CA TYR 475 29.824 27.812 50.376 1.00 21.74 1DLC3498 ATOM 3375 C TYR 475 29.081 27.125 49.244 1.00 20.48 1DLC3499 ATOM 3376 O TYR 475 29.219 27.472 48.069 1.00 18.90 1DLC3500 ATOM 3377 CB TYR 475 28.922 28.910 50.958 1.00 22.80 1DLC3501 ATOM 3378 CG TYR 475 28.050 28.481 52.117 1.00 23.56 1DLC3502 ATOM 3379 CD1 TYR 475 28.601 28.258 53.379 1.00 27.52 1DLC3503 ATOM 3380 CD2 TYR 475 26.672 28.324 51.963 1.00 23.00 1DLC3504 ATOM 3381 CE1 TYR 475 27.802 27.895 54.464 1.00 26.40 1DLC3505 ATOM 3382 CE2 TYR 475 25.858 27.958 53.043 1.00 24.16 1DLC3506 ATOM 3383 CZ TYR 475 26.430 27.746 54.291 1.00 25.06 1DLC3507 ATOM 3384 OH TYR 475 25.643 27.405 55.375 1.00 26.34 1DLC3508 ATOM 3385 N VAL 476 28.273 26.150 49.638 1.00 21.63 1DLC3509 ATOM 3386 CA VAL 476 27.444 25.379 48.724 1.00 22.28 1DLC3510 ATOM 3387 C VAL 476 26.046 25.309 49.355 1.00 23.25 1DLC3511 ATOM 3388 O VAL 476 25.905 25.032 50.546 1.00 22.42 1DLC3512 ATOM 3389 CB VAL 476 28.026 23.958 48.499 1.00 19.04 1DLC3513 ATOM 3390 CG1 VAL 476 27.025 23.077 47.813 1.00 20.37 1DLC3514 ATOM 3391 CG2 VAL 476 29.269 24.040 47.640 1.00 20.33 1DLC3515 ATOM 3392 N MET 477 25.026 25.652 48.575 1.00 22.47 1DLC3516 ATOM 3393 CA MET 477 23.655 25.627 49.069 1.00 22.92 1DLC3517 ATOM 3394 C MET 477 22.722 25.110 47.973 1.00 23.63 1DLC3518 ATOM 3395 O MET 477 22.819 25.531 46.825 1.00 24.06 1DLC3519 ATOM 3396 CB MET 477 23.246 27.030 49.517 1.00 24.95 1DLC3520 ATOM 3397 CG MET 477 22.027 27.076 50.408 1.00 34.31 1DLC3521 ATOM 3398 SD MET 477 21.578 28.761 50.913 1.00 36.69 1DLC3522 ATOM 3399 CE MET 477 22.689 29.016 52.281 1.00 38.04 1DLC3523 ATOM 3400 N CYS 478 21.870 24.150 48.327 1.00 25.18 1DLC3524 ATOM 3401 CA CYS 478 20.912 23.551 47.390 1.00 23.36 1DLC3525 ATOM 3402 C CYS 478 19.507 24.106 47.568 1.00 23.41 1DLC3526 ATOM 3403 O CYS 478 18.970 24.102 48.673 1.00 23.01 1DLC3527 ATOM 3404 CB CYS 478 20.843 22.029 47.564 1.00 21.73 1DLC3528 ATOM 3405 SG CYS 478 22.219 21.086 46.881 1.00 24.07 1DLC3529 ATOM 3406 N PHE 479 18.918 24.585 46.481 1.00 21.93 1DLC3530 ATOM 3407 CA PHE 479 17.563 25.118 46.513 1.00 19.16 1DLC3531 ATOM 3408 C PHE 479 16.629 24.149 45.814 1.00 20.36 1DLC3532 ATOM 3409 O PHE 479 17.032 23.431 44.897 1.00 19.20 1DLC3533 ATOM 3410 CB PHE 479 17.496 26.483 45.831 1.00 16.90 1DLC3534 ATOM 3411 CG PHE 479 18.194 27.563 46.592 1.00 19.07 1DLC3535 ATOM 3412 CD1 PHE 479 17.550 28.229 47.625 1.00 20.04 1DLC3536 ATOM 3413 CD2 PHE 479 19.509 27.891 46.308 1.00 17.03 1DLC3537 ATOM 3414 CE1 PHE 479 18.210 29.207 48.368 1.00 22.59 1DLC3538 ATOM 3415 CE2 PHE 479 20.173 28.866 47.044 1.00 23.10 1DLC3539 ATOM 3416 CZ PHE 479 19.525 29.524 48.075 1.00 18.71 1DLC3540 ATOM 3417 N LEU 480 15.384 24.102 46.269 1.00 21.81 1DLC3541 ATOM 3418 CA LEU 480 14.402 23.219 45.661 1.00 19.96 1DLC3542 ATOM 3419 C LEU 480 13.587 23.952 44.611 1.00 20.47 1DLC3543 ATOM 3420 O LEU 480 13.229 25.117 44.798 1.00 22.01 1DLC3544 ATOM 3421 CB LEU 480 13.474 22.629 46.719 1.00 16.36 1DLC3545 ATOM 3422 CG LEU 480 14.071 21.574 47.653 1.00 18.20 1DLC3546 ATOM 3423 CD1 LEU 480 13.045 21.170 48.675 1.00 16.09 1DLC3547 ATOM 3424 CD2 LEU 480 14.535 20.367 46.863 1.00 17.11 1DLC3548 ATOM 3425 N MET 481 13.375 23.300 43.473 1.00 19.08 1DLC3549 ATOM 3426 CA MET 481 12.557 23.875 42.411 1.00 21.22 1DLC3550 ATOM 3427 C MET 481 11.091 23.844 42.867 1.00 24.48 1DLC3551 ATOM 3428 O MET 481 10.729 23.084 43.772 1.00 25.50 1DLC3552 ATOM 3429 CB MET 481 12.674 23.055 41.133 1.00 18.69 1DLC3553 ATOM 3430 CG MET 481 14.002 23.129 40.458 1.00 20.79 1DLC3554 ATOM 3431 SD MET 481 13.988 22.032 39.060 1.00 25.38 1DLC3555 ATOM 3432 CE MET 481 15.738 21.837 38.753 1.00 21.04 1DLC3556 ATOM 3433 N GLN 482 10.251 24.662 42.241 1.00 25.74 1DLC3557 ATOM 3434 CA GLN 482 8.836 24.705 42.579 1.00 24.89 1DLC3558 ATOM 3435 C GLN 482 8.143 23.390 42.282 1.00 26.77 1DLC3559 ATOM 3436 O GLN 482 8.469 22.713 41.311 1.00 26.04 1DLC3560 ATOM 3437 CB GLN 482 8.153 25.834 41.840 1.00 22.45 1DLC3561 ATOM 3438 CG GLN 482 8.516 27.182 42.390 1.00 24.04 1DLC3562 ATOM 3439 CD GLN 482 7.592 28.241 41.888 1.00 25.93 1DLC3563 ATOM 3440 OE1 GLN 482 6.758 28.740 42.630 1.00 33.56 1DLC3564 ATOM 3441 NE2 GLN 482 7.697 28.565 40.617 1.00 24.90 1DLC3565 ATOM 3442 N GLY 483 7.200 23.017 43.141 1.00 31.29 1DLC3566 ATOM 3443 CA GLY 483 6.502 21.756 42.960 1.00 34.89 1DLC3567 ATOM 3444 C GLY 483 7.529 20.643 42.974 1.00 38.13 1DLC3568 ATOM 3445 O GLY 483 7.338 19.585 42.382 1.00 41.30 1DLC3569 ATOM 3446 N SER 484 8.644 20.928 43.639 1.00 40.46 1DLC3570 ATOM 3447 CA SER 484 9.781 20.027 43.760 1.00 39.19 1DLC3571 ATOM 3448 C SER 484 10.047 19.110 42.574 1.00 35.89 1DLC3572 ATOM 3449 O SER 484 9.982 17.891 42.682 1.00 34.78 1DLC3573 ATOM 3450 CB SER 484 9.716 19.258 45.070 1.00 44.00 1DLC3574 ATOM 3451 OG SER 484 9.864 20.160 46.158 1.00 49.80 1DLC3575 ATOM 3452 N ARG 485 10.322 19.728 41.430 1.00 34.10 1DLC3576 ATOM 3453 CA ARG 485 10.639 18.998 40.212 1.00 33.89 1DLC3577 ATOM 3454 C ARG 485 12.155 18.734 40.152 1.00 34.69 1DLC3578 ATOM 3455 O ARG 485 12.630 17.971 39.305 1.00 36.50 1DLC3579 ATOM 3456 CB ARG 485 10.197 19.800 38.983 1.00 33.16 1DLC3580 ATOM 3457 CG ARG 485 10.266 19.019 37.669 1.00 36.98 1DLC3581 ATOM 3458 CD ARG 485 9.882 19.889 36.485 1.00 41.59 1DLC3582 ATOM 3459 NE ARG 485 8.680 19.445 35.770 1.00 42.72 1DLC3583 ATOM 3460 CZ ARG 485 7.505 19.169 36.335 1.00 44.05 1DLC3584 ATOM 3461 NH1 ARG 485 7.332 19.265 37.647 1.00 44.99 1DLC3585 ATOM 3462 NH2 ARG 485 6.470 18.863 35.569 1.00 47.30 1DLC3586 ATOM 3463 N GLY 486 12.910 19.365 41.052 1.00 32.23 1DLC3587 ATOM 3464 CA GLY 486 14.352 19.174 41.068 1.00 29.57 1DLC3588 ATOM 3465 C GLY 486 15.115 20.016 42.078 1.00 28.60 1DLC3589 ATOM 3466 O GLY 486 14.511 20.692 42.919 1.00 25.84 1DLC3590 ATOM 3467 N THR 487 16.443 19.992 41.966 1.00 25.86 1DLC3591 ATOM 3468 A THR 487 17.337 20.732 42.862 1.00 24.67 1DLC3592 ATOM 3469 C THR 487 18.295 21.665 42.121 1.00 25.25 1DLC3593 ATOM 3470 O THR 487 18.962 21.260 41.164 1.00 25.06 1DLC3594 ATOM 3471 CB THR 487 18.183 19.760 43.728 1.00 25.40 1DLC3595 ATOM 3472 CG1 THR 487 17.344 19.141 44.707 1.00 26.03 1DLC3596 ATOM 3473 CG2 THR 487 19.320 20.487 44.438 1.00 26.87 1DLC3597 ATOM 3474 N ILE 488 18.370 22.909 42.584 1.00 22.95 1DLC3598 ATOM 3475 CA ILE 488 19.257 23.915 41.993 1.00 24.06 1DLC3599 ATOM 3476 C ILE 488 20.378 24.293 42.966 1.00 24.12 1DLC3600 ATOM 3477 O ILE 488 20.120 24.890 44.017 1.00 26.94 1DLC3601 ATOM 3478 CB ILE 488 18.496 25.214 41.633 1.00 22.37 1DLC3602 ATOM 3479 CG1 ILE 488 17.343 24.915 40.668 1.00 21.27 1DLC3603 ATOM 3480 CG2 ILE 488 19.456 26.225 41.020 1.00 16.51 1DLC3604 ATOM 3481 CD1 ILE 488 16.468 26.115 40.375 1.00 20.81 1DLC3605 ATOM 3482 N PRO 489 21.628 23.895 42.667 1.00 24.55 1DLC3606 ATOM 3483 CA PRO 489 22.741 24.239 43.567 1.00 22.62 1DLC3607 ATOM 3484 C PRO 489 23.285 25.646 43.290 1.00 20.82 1DLC3608 ATOM 3485 O PRO 489 23.321 26.094 42.137 1.00 22.41 1DLC3609 ATOM 3486 CB PRO 489 23.797 23.175 43.240 1.00 20.03 1DLC3610 ATOM 3487 CG PRO 489 23.028 22.083 42.522 1.00 22.59 1DLC3611 ATOM 3488 CD PRO 489 22.052 22.876 41.695 1.00 20.82 1DLC3612 ATOM 3489 N VAL 490 23.663 26.348 44.353 1.00 18.80 1DLC3613 ATOM 3490 CA VAL 490 24.234 27.686 44.241 1.00 20.56 1DLC3614 ATOM 3491 C VAL 490 25.539 27.745 45.045 1.00 22.82 1DLC3615 ATOM 3492 O VAL 490 25.576 27.364 46.225 1.00 20.83 1DLC3616 ATOM 3493 CB VAL 490 23.257 28.772 44.732 1.00 22.17 1DLC3617 ATOM 3494 CG1 VAL 490 23.899 30.147 44.621 1.00 20.36 1DLC3618 ATOM 3495 CG2 VAL 490 21.989 28.740 43.895 1.00 24.80 1DLC3619 ATOM 3496 N LEU 491 26.610 28.206 44.397 1.00 22.64 1DLC3620 ATOM 3497 CA LEU 491 27.931 28.285 45.034 1.00 21.56 1DLC3621 ATOM 3498 C LEU 491 28.397 29.704 45.377 1.00 19.56 1DLC3622 ATOM 3499 O LEU 491 28.279 30.622 44.566 1.00 21.15 1DLC3623 ATOM 3500 CB LEU 491 28.993 27.610 44.143 1.00 22.96 1DLC3624 ATOM 3501 CG LEU 491 28.739 26.213 43.549 1.00 22.44 1DLC3625 ATOM 3502 CD1 LEU 491 29.970 25.728 42.817 1.00 19.64 1DLC3626 ATOM 3503 CD2 LEU 491 28.359 25.222 44.617 1.00 23.77 1DLC3627 ATOM 3504 N THR 492 28.926 29.867 46.584 1.00 17.65 1DLC3628 ATOM 3505 CA THR 492 29.451 31.153 47.050 1.00 21.18 1DLC3629 ATOM 3506 C THR 492 30.987 31.103 47.093 1.00 24.42 1DLC3630 ATOM 3507 O THR 492 31.580 30.111 47.545 1.00 25.76 1DLC3631 ATOM 3508 CB THR 492 28.927 31.503 48.451 1.00 20.37 1DLC3632 ATOM 3509 OG1 THR 492 27.498 31.509 48.419 1.00 25.73 1DLC3633 ATOM 3510 CG2 THR 492 29.421 32.881 48.898 1.00 16.18 1DLC3634 ATOM 3511 N TRP 493 31.622 32.184 46.638 1.00 23.37 1DLC3635 ATOM 3512 CA TRP 493 33.081 32.278 46.582 1.00 20.05 1DLC3636 ATOM 3513 C TRP 493 33.650 33.491 47.311 1.00 19.63 1DLC3637 ATOM 3514 O TRP 493 32.953 34.468 47.561 1.00 20.47 1DLC3638 ATOM 3515 CB TRP 493 33.546 32.333 45.123 1.00 16.78 1DLC3639 ATOM 3516 CG TRP 493 32.986 31.242 44.273 1.00 20.23 1DLC3640 ATOM 3517 CD1 TRP 493 31.692 31.113 43.852 1.00 19.07 1DLC3641 ATOM 3518 CD2 TRP 493 33.699 30.128 43.723 1.00 22.53 1DLC3642 ATOM 3519 NE1 TRP 493 31.555 29.991 43.075 1.00 19.83 1DLC3643 ATOM 3520 CE2 TRP 493 32.770 29.367 42.975 1.00 22.55 1DLC3644 ATOM 3521 CE3 TRP 493 35.033 29.699 43.785 1.00 24.17 1DLC3645 ATOM 3522 CZ2 TRP 493 33.132 28.198 42.294 1.00 22.22 1DLC3646 ATOM 3523 CZ3 TRP 493 35.394 28.536 43.107 1.00 21.82 1DLC3647 ATOM 3524 CH2 TRP 493 34.443 27.800 42.372 1.00 23.98 1DLC3648 ATOM 3525 N THR 494 34.930 33.402 47.661 1.00 19.10 1DLC3649 ATOM 3526 CA THR 494 35.643 34.488 48.323 1.00 15.75 1DLC3650 ATOM 3527 C THR 494 36.962 34.781 47.583 1.00 15.71 1DLC3651 ATOM 3528 O THR 494 37.497 33.923 46.885 1.00 15.53 1DLC3652 ATOM 3529 CB THR 494 35.867 34.199 49.832 1.00 17.76 1DLC3653 ATOM 3530 OG1 THR 494 36.483 32.913 50.007 1.00 18.92 1DLC3654 ATOM 3531 CG2 THR 494 34.530 34.232 50.580 1.00 13.45 1DLC3655 ATOM 3532 N HIS 495 37.448 36.011 47.679 1.00 17.73 1DLC3656 ATOM 3533 CA HIS 495 38.670 36.416 46.992 1.00 18.64 1DLC3657 ATOM 3534 C HIS 495 39.964 35.767 47.516 1.00 21.22 1DLC3658 ATOM 3535 O HIS 495 40.139 35.531 48.712 1.00 19.11 1DLC3659 ATOM 3536 CB HIS 495 38.788 37.953 46.991 1.00 18.90 1DLC3660 ATOM 3537 CG HIS 495 39.689 38.498 45.923 1.00 18.38 1DLC3661 ATOM 3538 ND1 HIS 495 41.018 38.801 46.147 1.00 20.90 1DLC3662 ATOM 3539 CD2 HIS 495 39.454 38.800 44.624 1.00 19.10 1DLC3663 ATOM 3540 CE1 HIS 495 41.559 39.261 45.035 1.00 19.17 1DLC3664 ATOM 3541 NE2 HIS 495 40.631 39.272 44.096 1.00 18.99 1DLC3665 ATOM 3542 N LYS 496 40.861 35.489 46.576 1.00 23.22 1DLC3666 ATOM 3543 CA LYS 496 42.171 34.876 46.818 1.00 25.84 1DLC3667 ATOM 3544 C LYS 496 43.103 35.666 47.755 1.00 26.33 1DLC3668 ATOM 3545 O LYS 496 43.986 35.095 48.388 1.00 26.36 1DLC3669 ATOM 3546 CB LYS 496 42.853 34.711 45.462 1.00 27.94 1DLC3670 ATOM 3547 CG LYS 496 44.251 34.139 45.447 1.00 28.83 1DLC3671 ATOM 3548 CD LYS 496 44.885 34.574 44.138 1.00 31.25 1DLC3672 ATOM 3549 CE LYS 496 46.050 33.721 43.720 1.00 30.77 1DLC3673 ATOM 3550 NZ LYS 496 46.516 34.187 42.380 1.00 37.65 1DLC3674 ATOM 3551 N SER 497 42.900 36.977 47.834 1.00 25.35 1DLC3675 ATOM 3552 CA SER 497 43.741 37.838 48.660 1.00 22.15 1DLC3676 ATOM 3553 C SER 497 43.607 37.644 50.152 1.00 22.22 1DLC3677 ATOM 3554 O SER 497 44.460 38.105 50.904 1.00 25.41 1DLC3678 ATOM 3555 CB SER 497 43.486 39.306 48.342 1.00 23.23 1DLC3679 ATOM 3556 OG SER 497 42.133 39.656 48.583 1.00 22.68 1DLC3680 ATOM 3557 N VAL 498 42.526 37.002 50.585 1.00 23.61 1DLC3681 ATOM 3558 CA VAL 498 42.293 36.777 52.013 1.00 20.99 1DLC3682 ATOM 3559 C VAL 498 43.379 35.909 52.659 1.00 21.85 1DLC3683 ATOM 3560 O VAL 498 43.637 34.783 52.229 1.00 23.91 1DLC3684 ATOM 3561 CB VAL 498 40.877 36.180 52.285 1.00 21.37 1DLC3685 ATOM 3562 CG1 VAL 498 40.688 35.932 53.777 1.00 21.12 1DLC3686 ATOM 3563 CG2 VAL 498 39.788 37.139 51.787 1.00 17.66 1DLC3687 ATOM 3564 N ASP 499 44.029 36.467 53.675 1.00 19.96 1DLC3688 ATOM 3565 CA ASP 499 45.101 35.801 54.408 1.00 16.56 1DLC3689 ATOM 3566 C ASP 499 44.551 35.050 55.623 1.00 17.05 1DLC3690 ATOM 3567 O ASP 499 44.184 35.659 56.619 1.00 17.65 1DLC3691 ATOM 3568 CB ASP 499 46.145 36.853 54.834 1.00 18.86 1DLC3692 ATOM 3569 CG ASP 499 47.238 36.290 55.750 1.00 20.23 1DLC3693 ATOM 3570 OD1 ASP 499 47.451 35.066 55.786 1.00 28.20 1DLC3694 ATOM 3571 OD2 ASP 499 47.903 37.079 56.440 1.00 20.77 1DLC3695 ATOM 3572 N PHE 500 44.555 33.724 55.561 1.00 18.66 1DLC3696 ATOM 3573 CA PHE 500 44.049 32.924 56.668 1.00 21.20 1DLC3697 ATOM 3574 C PHE 500 44.725 33.213 57.994 1.00 21.18 1DLC3698 ATOM 3575 O PHE 500 44.083 33.205 59.039 1.00 23.89 1DLC3699 ATOM 3576 CB PHE 500 44.167 31.416 56.391 1.00 24.40 1DLC3700 ATOM 3577 CG PHE 500 43.787 30.552 57.587 1.00 27.73 1DLC3701 ATOM 3578 CD1 PHE 500 42.445 30.306 57.890 1.00 27.36 1DLC3702 ATOM 3579 CD2 PHE 500 44.768 30.044 58.445 1.00 26.00 1DLC3703 ATOM 3580 CE1 PHE 500 42.084 29.578 59.026 1.00 25.15 1DLC3704 ATOM 3581 CE2 PHE 500 44.417 29.316 59.583 1.00 26.25 1DLC3705 ATOM 3582 CZ PHE 500 43.070 29.084 59.874 1.00 25.99 1DLC3706 ATOM 3583 N PHE 501 46.027 33.443 57.959 1.00 21.02 1DLC3707 ATOM 3584 CA PHE 501 46.767 33.685 59.191 1.00 21.95 1DLC3708 ATOM 3585 C PHE 501 46.673 35.047 59.877 1.00 20.32 1DLC3709 ATOM 3586 O PHE 501 47.173 35.189 60.986 1.00 20.00 1DLC3710 ATOM 3587 CB PHE 501 48.234 33.285 59.001 1.00 25.51 1DLC3711 ATOM 3588 CG PHE 501 48.419 31.823 58.707 1.00 24.22 1DLC3712 ATOM 3589 CD1 PHE 501 48.383 30.887 59.733 1.00 24.19 1DLC3713 ATOM 3590 CD2 PHE 501 48.589 31.380 57.403 1.00 25.81 1DLC3714 ATOM 3591 CE1 PHE 501 48.510 29.536 59.467 1.00 23.35 1DLC3715 ATOM 3592 CE2 PHE 501 48.717 30.027 57.125 1.00 24.04 1DLC3716 ATOM 3593 CZ PHE 501 48.677 29.104 58.160 1.00 23.29 1DLC3717 ATOM 3594 N ASN 502 46.005 36.024 59.256 1.00 21.94 1DLC3718 ATOM 3595 CA ASN 502 45.881 37.378 59.828 1.00 18.99 1DLC3719 ATOM 3596 C ASN 502 47.281 37.834 60.228 1.00 19.72 1DLC3720 ATOM 3597 O ASN 502 47.530 38.238 61.359 1.00 21.21 1DLC3721 ATOM 3598 CB ASN 502 44.959 37.375 61.061 1.00 19.98 1DLC3722 ATOM 3599 CG ASN 502 43.470 37.293 60.703 1.00 18.11 1DLC3723 ATOM 3600 OD1 ASN 502 43.079 37.424 59.544 1.00 14.73 1DLC3724 ATOM 3601 ND2 ASN 502 42.639 37.089 61.712 1.00 11.25 1DLC3725 ATOM 3602 N MET 503 48.197 37.741 59.278 1.00 22.71 1DLC3726 ATOM 3603 CA MET 503 49.590 38.071 59.509 1.00 24.59 1DLC3727 ATOM 3604 C MET 503 49.958 39.5A4 59.415 1.00 26.15 1DLC3728 ATOM 3605 O MET 503 49.705 40.199 58.402 1.00 24.32 1DLC3729 ATOM 3606 CB MET 503 50.456 37.245 58.565 1.00 31.72 1DLC3730 ATOM 3607 CG MET 503 51.918 37.179 58.939 1.00 43.44 1DLC3731 ATOM 3608 SD MET 503 52.748 35.901 57.973 1.00 55.24 1DLC3732 ATOM 3609 CE MET 503 52.027 34.424 58.732 1.00 51.41 1DLC3733 ATOM 3610 N ILE 504 50.583 40.042 60.482 1.00 26.22 1DLC3734 ATOM 3611 CA ILE 504 51.026 41.433 60.575 1.00 27.43 1DLC3735 ATOM 3612 C ILE 504 52.423 41.578 59.966 1.00 30.21 1DLC3736 ATOM 3613 O ILE 504 53.419 41.149 60.557 1.00 31.93 1DLC3737 ATOM 3614 CB ILE 504 51.048 41.912 62.050 1.00 25.85 1DLC3738 ATOM 3615 CG1 ILE 504 49.702 41.626 62.707 1.00 24.52 1DLC3739 ATOM 3616 CG2 ILE 504 51.336 43.401 62.129 1.00 24.26 1DLC3740 ATOM 3617 CD1 ILE 504 48.522 42.137 61.919 1.00 25.27 1DLC3741 ATOM 3618 N ASP 505 52.483 42.169 58.776 1.00 32.77 1DLC3742 ATOM 3619 CA ASP 505 53.740 42.371 58.055 1.00 32.61 1DLC3743 ATOM 3620 C ASP 505 54.658 43.386 58.737 1.00 33.24 1DLC3744 ATOM 3621 O ASP 505 54.243 44.501 59.034 1.00 37.00 1DLC3745 ATOM 3622 CB ASP 505 53.454 42.828 56.629 1.00 33.22 1DLC3746 ATOM 3623 CG ASP 505 54.639 42.636 55.715 1.00 35.54 1DLC3747 ATOM 3624 OD1 ASP 505 55.606 43.413 55.804 1.00 40.96 1DLC3748 ATOM 3625 OD2 ASP 505 54.612 41.694 54.903 1.00 39.21 1DLC3749 ATOM 3626 N SER 506 55.924 43.018 58.910 1.00 33.99 1DLC3750 ATOM 3627 CA SER 506 56.916 43.878 59.569 1.00 31.14 1DLC3751 ATOM 3628 C SER 506 57.433 45.058 58.753 1.00 26.45 1DLC3752 ATOM 3629 O SER 506 58.091 45.932 59.296 1.00 25.94 1DLC3753 ATOM 3630 CB SER 506 58.116 43.049 60.035 1.00 35.65 1DLC3754 ATOM 3631 OG SER 506 58.691 42.318 58.955 1.00 38.49 1DLC3755 ATOM 3632 N LYS 507 57.181 45.064 57.452 1.00 24.25 1DLC3756 ATOM 3633 CA LYS 507 57.653 46.155 56.603 1.00 29.55 1DLC3757 ATOM 3634 C LYS 507 56.540 47.011 56.016 1.00 29.60 1DLC3758 ATOM 3635 O LYS 507 56.773 48.150 55.611 1.00 30.94 1DLC3759 ATOM 3636 CB LYS 507 58.494 45.630 55.435 1.00 34.60 1DLC3760 ATOM 3637 CG LYS 507 59.661 44.732 55.793 1.00 44.16 1DLC3761 ATOM 3638 CD LYS 507 59.206 43.295 56.004 1.00 54.27 1DLC3762 ATOM 3639 CE LYS 507 60.303 42.327 55.603 1.00 60.68 1DLC3763 ATOM 3640 NZ LYS 507 60.686 42.532 54.163 1.00 64.19 1DLC3764 ATOM 3641 N LYS 508 55.339 46.452 55.942 1.00 28.18 1DLC3765 ATOM 3642 CA LYS 508 54.204 47.165 55.364 1.00 24.79 1DLC3766 ATOM 3643 C LYS 508 53.175 47.608 56.378 1.00 23.56 1DLC3767 ATOM 3644 O LYS 508 53.248 47.273 57.563 1.00 25.61 1DLC3768 ATOM 3645 CB LYS 508 53.480 46.273 54.359 1.00 21.88 1DLC3769 ATOM 3646 CG LYS 508 54.329 45.804 53.233 1.00 25.15 1DLC3770 ATOM 3647 CD LYS 508 53.592 44.816 52.383 1.00 26.67 1DLC3771 ATOM 3648 CE LYS 508 54.495 44.343 51.263 1.00 31.83 1DLC3772 ATOM 3649 NZ LYS 508 53.858 43.338 50.378 1.00 35.43 1DLC3773 ATOM 3650 N ILE 509 52.239 48.413 55.900 1.00 20.93 1DLC3774 ATOM 3651 CA ILE 509 51.121 48.837 56.715 1.00 18.88 1DLC3775 ATOM 3652 C ILE 509 50.137 47.695 56.446 1.00 19.04 1DLC3776 ATOM 3653 O ILE 509 49.887 47.333 55.293 1.00 17.01 1DLC3777 ATOM 3654 CB ILE 509 50.539 50.186 56.236 1.00 18.64 1DLC3778 ATOM 3655 CG1 ILE 509 51.530 51.317 56.558 1.00 14.90 1DLC3779 ATOM 3656 CG2 ILE 509 49.157 50.421 56.872 1.00 15.43 1DLC3780 ATOM 3657 CD1 ILE 509 51.149 52.677 56.007 1.00 11.51 1DLC3781 ATOM 3658 N THR 510 49.674 47.052 57.506 1.00 21.46 1DLC3782 ATOM 3659 CA THR 510 48.751 45.931 57.358 1.00 20.67 1DLC3783 ATOM 3660 C THR 510 47.309 46.291 57.709 1.00 19.90 1DLC3784 ATOM 3661 O THR 510 47.034 46.781 58.806 1.00 23.72 1DLC3785 ATOM 3662 CB THR 510 49.181 44.726 58.253 1.00 20.85 1DLC3786 ATOM 3663 OG1 THR 510 50.522 44.326 57.929 1.00 20.93 1DLC3787 ATOM 3664 CG2 THR 510 48.241 43.541 58.051 1.00 21.70 1DLC3788 ATOM 3665 N GLN 511 46.399 46.087 56.763 1.00 18.34 1DLC3789 ATOM 3666 CA GLN 511 44.979 46.336 57.001 1.00 16.87 1DLC3790 ATOM 3667 C GLN 511 44.283 45.037 57.428 1.00 20.95 1DLC3791 ATOM 3668 O GLN 511 44.281 44.048 56.689 1.00 22.60 1DLC3792 ATOM 3669 CB GLN 511 44.293 46.868 55.748 1.00 12.52 1DLC3793 ATOM 3670 CG GLN 511 44.506 48.332 55.481 1.00 14.00 1DLC3794 ATOM 3671 CD GLN 511 43.533 48.867 54.440 1.00 18.99 1DLC3795 ATOM 3672 OE1 GLN 511 43.290 48.236 53.417 1.00 21.33 1DLC3796 ATOM 3673 NE2 GLN 511 42.956 50.018 54.708 1.00 19.00 1DLC3797 ATOM 3674 N LEU 512 43.710 45.043 58.626 1.00 22.52 1DLC3798 ATOM 3675 CA LEU 512 42.989 43.889 59.162 1.00 21.75 1DLC3799 ATOM 3676 C LEU 512 41.480 44.130 59.277 1.00 19.63 1DLC3800 ATOM 3677 O LEU 512 41.023 44.839 60.175 1.00 19.45 1DLC3801 ATOM 3678 CB LEU 512 43.522 43.518 60.546 1.00 25.44 1DLC3802 ATOM 3679 CG LEU 512 44.431 42.303 60.672 1.00 32.43 1DLC3803 ATOM 3680 CD1 LEU 512 44.559 41.951 62.148 1.00 32.49 1DLC3804 ATOM 3681 CD2 LEU 512 43.843 41.128 59.892 1.00 35.48 1DLC3805 ATOM 3682 N PRO 513 40.685 43.537 58.372 1.00 17.33 1DLC3806 ATOM 3683 CA PRO 513 39.227 43.700 58.402 1.00 16.04 1DLC3807 ATOM 3684 C PRO 513 38.669 43.052 59.662 1.00 15.65 1DLC3808 ATOM 3685 O PRO 513 39.043 41.933 59.993 1.00 19.58 1DLC3809 ATOM 3686 CB PRO 513 38.776 42.934 57.163 1.00 12.95 1DLC3810 ATOM 3687 CG PRO 513 39.964 43.01T 56.253 1.00 16.06 1DLC3811 ATOM 3688 CD PRO 513 41.096 42.757 57.195 1.00 16.99 1DLC3812 ATOM 3689 N LEU 514 37.775 43.742 60.361 1.00 17.11 IDLC3813 ATOM 3690 CA LEU 514 37.187 43.195 61.584 1.00 17.00 1DLC3814 ATOM 3691 C LEU 514 36.391 41.896 61.390 1.00 16.47 1DLC3815 ATOM 3692 O LEU 514 36.222 41.115 62.334 1.00 15.86 1DLC3816 ATOM 3693 CB LEU 514 36.324 44.249 62.279 1.00 20.38 1DLC3817 ATOM 3694 CG LEU 514 36.962 44.901 63.512 1.00 24.64 1DLC3818 ATOM 3695 CD1 LEU 514 37.104 43.877 64.633 1.00 22.36 1DLC3819 ATOM 3696 CD2 LEU 514 38.319 45.500 63.156 1.00 26.24 1DLC3820 ATOM 3697 N VAL 515 35.888 41.668 60.179 1.00 13.44 1DLC3821 ATOM 3698 CA VAL 515 35.147 40.443 59.906 1.00 17.69 1DLC3822 ATOM 3699 C VAL 515 36.038 39.200 59.983 1.00 19.77 1DLC3823 ATOM 3700 O VAL 515 35.541 38.082 59.927 1.00 21.83 1DLC3824 ATOM 3701 CB VAL 515 34.382 40.476 58.546 1.00 15.76 1DLC3825 ATOM 3702 CG1 VAL 515 33.316 41.552 58.584 1.00 15.76 1DLC3826 ATOM 3703 CG2 VAL 515 35.326 40.693 57.386 1.00 13.28 1DLC3827 ATOM 3704 N LYS 516 37.351 39.405 60.106 1.00 22.24 1DLC3828 ATOM 3705 CA LYS 516 38.311 38.304 60.233 1.00 20.87 1DLC3829 ATOM 3706 C LYS 516 38.405 37.867 61.704 1.00 21.16 1DLC3830 ATOM 3707 O LYS 516 39.164 36.967 62.059 1.00 22.50 1DLC3831 ATOM 3708 CB LYS 516 39.692 38.716 59.717 1.00 19.84 1DLC3832 ATOM 3709 CG LYS 516 39.768 39.001 58.211 1.00 19.10 1DLC3833 ATOM 3710 CD LYS 516 39.499 37.756 57.361 1.00 18.48 1DLC3834 ATOM 3711 CE LYS 516 40.581 36.692 57.519 1.00 19.98 1DLC3835 ATOM 3712 NZ LYS 516 41.938 37.189 57.136 1.00 18.44 1DLC3836 ATOM 3713 N ALA 517 37.652 38.534 62.568 1.00 19.22 1DLC3837 ATOM 3714 CA ALA 517 37.631 38.173 63.972 1.00 18.13 1DLC3838 ATOM 3715 C ALA 517 37.037 36.769 64.075 1.00 18.92 1DLC3839 ATOM 3716 O ALA 517 36.396 36.277 63.141 1.00 21.52 1DLC3840 ATOM 3717 CB ALA 517 36.782 39.171 64.759 1.00 12.71 1DLC3841 ATOM 3718 N TYR 518 37.289 36.093 65.183 1.00 21.01 1DLC3842 ATOM 3719 CA TYR 518 36.728 34.759 65.364 1.00 23.07 1DLC3843 ATOM 3720 C TYR 518 35.657 34.785 66.451 1.00 24.25 1DLC3844 ATOM 3721 O TYR 518 34.881 33.846 66.592 1.00 28.06 1DLC3845 ATOM 3722 CB TYR 518 37.824 33.743 65.716 1.00 19.73 1DLC3846 ATOM 3723 CG TYR 518 38.472 33.952 67.065 1.00 19.33 1DLC3847 ATOM 3724 CD1 TYR 518 37.888 33.442 68.229 1.00 22.01 1DLC3848 ATOM 3725 CD2 TYR 518 39.676 34.644 67.180 1.00 19.86 1DLC3849 ATOM 3726 CE1 TYR 518 38.485 33.611 69.471 1.00 18.79 1DLC3850 ATOM 3727 CE2 TYR 518 40.283 34.823 68.417 1.00 20.61 1DLC3851 ATOM 3728 CZ TYR 518 39.682 34.304 69.557 1.00 22.78 1DLC3852 ATOM 3729 OH TYR 518 40.270 34.493 70.783 1.00 24.17 1DLC3853 ATOM 3730 N LYS 519 35.564 35.905 67.160 1.00 24.18 1DLC3854 ATOM 3731 CA LYS 519 34.615 36.027 68.249 1.00 21.87 1DLC3855 ATOM 3732 C LYS 519 34.027 37.429 68.430 1.00 22.52 1DLC3856 ATOM 3733 O LYS 519 34.758 38.410 68.527 1.00 22.87 1DLC3857 ATOM 3734 CB LYS 519 35.328 35.593 69.526 1.00 24.86 1DLC3858 ATOM 3735 CG LYS 519 34.512 35.599 70.783 1.00 31.39 1DLC3859 ATOM 3736 CD LYS 519 35.400 35.210 71.953 1.00 38.43 1DLC3860 ATOM 3737 CE LYS 519 34.616 35.118 73.255 1.00 45.64 1DLC3861 ATOM 3738 NZ LYS 519 35.523 34.808 74.400 1.00 49.23 1DLC3862 ATOM 3739 N LEU 520 32.703 37.522 68.422 1.00 21.94 1DLC3863 ATOM 3740 CA LEU 520 32.024 38.794 68.653 1.00 24.06 1DLC3864 ATOM 3741 C LEU 520 31.408 38.738 70.050 1.00 27.63 1DLC3865 ATOM 3742 O LEU 520 31.091 37.660 70.556 1.00 29.95 1DLC3866 ATOM 3743 CB LEU 520 30.943 39.063 67.600 1.00 20.93 1DLC3867 ATOM 3744 CG LEU 520 31.438 39.461 66.209 1.00 21.24 1DLC3868 ATOM 3745 CD1 LEU 520 30.268 39.640 65.274 1.00 21.64 1DLC3869 ATOM 3746 CD2 LEU 520 32.252 40.744 66.292 1.00 20.28 1DLC3870 ATOM 3747 N GLN 521 31.214 39.894 70.668 1.00 30.71 1DLC3871 ATOM 3748 CA GLN 521 30.667 39.935 72.015 1.00 32.68 1DLC3872 ATOM 3749 C GLN 521 29.943 41.237 72.338 1.00 32.85 1DLC3873 ATOM 3750 O GLN 521 29.963 42.183 71.554 1.00 33.06 1DLC3874 ATOM 3751 CB GLN 521 31.795 39.681 73.019 1.00 38.17 1DLC3875 ATOM 3752 CG GLN 521 33.040 40.525 72.764 1.00 47.16 1DLC3876 ATOM 3753 CD GLN 521 34.341 39.733 72.860 1.00 50.53 1DLC3877 ATOM 3754 OE1 GLN 521 34.416 38.715 73.546 1.00 53.19 1DLC3878 ATOM 3755 NE2 GLN 521 35.372 40.205 72.171 1.00 49.13 1DLC3879 ATOM 3756 N SER 522 29.284 41.261 73.494 1.00 34.02 1DLC3880 ATOM 3757 CA SER 522 28.529 42.427 73.963 1.00 33.25 1DLC3881 ATOM 3758 C SER 522 27.458 42.871 72.973 1.00 32.49 1DLC3882 ATOM 3759 O SER 522 27.132 44.051 72.887 1.00 34.90 1DLC3883 ATOM 3760 CB SER 522 29.464 43.607 74.267 1.00 34.44 1DLC3884 ATOM 3761 OG SER 522 30.460 43.269 75.221 1.00 37.23 1DLC3885 ATOM 3762 N GLY 523 26.932 41.931 72.201 1.00 32.83 1DLC3886 ATOM 3763 CA GLY 523 25.906 42.283 71.236 1.00 35.47 1DLC3887 ATOM 3764 C GLY 523 26.415 42.914 69.946 1.00 37.76 1DLC3888 ATOM 3765 O GLY 523 25.694 43.676 69.291 1.00 43.56 1DLC3889 ATOM 3766 N ALA 524 27.675 42.662 69.606 1.00 33.37 1DLC3890 ATOM 3767 CA ALA 524 28.228 43.181 68.366 1.00 25.62 1DLC3891 ATOM 3768 C ALA 524 27.772 42.233 67.254 1.00 25.43 1DLC3892 ATOM 3769 O ALA 524 27.507 41.054 67.501 1.00 25.41 1DLC3893 ATOM 3770 CB ALA 524 29.742 43.232 68.443 1.00 22.42 1DLC3894 ATOM 3771 N SER 525 27.648 42.738 66.035 1.00 24.40 1DLC3895 ATOM 3772 CA SER 525 27.224 41.887 64.927 1.00 22.01 1DLC3896 ATOM 3773 C SER 525 27.755 42.326 63.571 1.00 19.44 1DLC3897 ATOM 3774 O SER 525 28.125 43.479 63.380 1.00 21.43 1DLC3898 ATOM 3775 CB SER 525 25.702 41.820 64.863 1.00 21.54 1DLC3899 ATOM 3776 OG SER 525 25.147 43.092 64.593 1.00 25.37 1DLC3900 ATOM 3777 N VAL 526 27.797 41.387 62.634 1.00 19.65 1DLC3901 ATOM 3778 CA VAL 526 28.261 41.669 61.282 1.00 16.70 1DLC3902 ATOM 3779 C VAL 526 27.096 42.274 60.519 1.00 19.66 1DLC3903 ATOM 3780 O VAL 526 25.986 41.742 60.522 1.00 25.06 1DLC3904 ATOM 3781 CB VAL 526 28.753 40.403 60.562 1.00 14.06 1DLC3905 ATOM 3782 CG1 VAL 526 29.368 40.763 59.211 1.00 11.22 1DLC3906 ATOM 3783 CG2 VAL 526 29.761 39.676 61.436 1.00 14.41 1DLC3907 ATOM 3784 N VAL 527 27.365 43.390 59.863 1.00 19.37 1DLC3908 ATOM 3785 CA VAL 527 26.361 44.119 59.116 1.00 15.54 1DLC3909 ATOM 3786 C VAL 527 26.834 44.303 57.672 1.00 15.70 1DLC3910 ATOM 3787 O VAL 527 28.034 44.247 57.392 1.00 17.61 1DLC3911 ATOM 3788 CB VAL 527 26.098 45.469 59.854 1.00 17.86 1DLC3912 ATOM 3789 CG1 VAL 527 25.762 46.576 58.907 1.00 23.79 1DLC3913 ATOM 3790 CG2 VAL 527 24.983 45.294 60.864 1.00 15.07 1DLC3914 ATOM 3791 N ALA 528 25.887 44.454 56.751 1.00 14.37 1DLC3915 ATOM 3792 CA ALA 528 26.204 A4.644 55.340 1.00 15.60 1DLC3916 ATOM 3793 C ALA 528 27.117 45.844 55.173 1.00 18.07 1DLC3917 ATOM 3794 O ALA 528 26.894 46.890 55.775 1.00 20.56 1DLC3918 ATOM 3795 CB ALA 528 24.937 44.838 54.531 1.00 12.04 1DLC3919 ATOM 3796 N GLY 529 28.152 45.687 54.361 1.00 18.47 1DLC3920 ATOM 3797 CA GLY 529 29.081 46.778 54.165 1.00 19.29 1DLC3921 ATOM 3798 C GLY 529 28.491 47.865 53.305 1.00 19.15 1DLC3922 ATOM 3799 O GLY 529 27.583 47.595 52.518 1.00 21.01 1DLC3923 ATOM 3800 N PRO 530 29.007 49.101 53.404 1.00 18.13 1DLC3924 ATOM 3801 CA PRO 530 28.519 50.239 52.618 1.00 16.51 1DLC3925 ATOM 3802 C PRO 530 28.840 50.175 51.112 1.00 16.39 1DLC3926 ATOM 3803 O PRO 530 28.610 51.139 50.386 1.00 17.87 1DLC3927 ATOM 3804 CB PRO 530 29.177 51.434 53.313 1.00 15.38 1DLC3928 ATOM 3805 CG PRO 530 30.462 50.873 53.810 1.00 15.73 1DLC3929 ATOM 3806 CD PRO 530 30.048 49.526 54.357 1.00 17.90 1DLC3930 ATOM 3807 N ARG 531 29.347 49.024 50.660 1.00 15.80 1DLC3931 ATOM 3808 CA ARG 531 29.705 48.743 49.260 1.00 16.70 1DLC3932 ATOM 3809 C ARG 531 31.048 49.293 48.778 1.00 18.92 1DLC3933 ATOM 3810 O ARG 531 31.478 48.985 47.672 1.00 23.34 1DLC3934 ATOM 3811 CB ARG 531 28.603 49.164 48.270 1.00 19.92 1DLC3935 ATOM 3812 CG ARG 531 27.162 48.685 48.568 1.00 28.20 1DLC3936 ATOM 3813 CD ARG 531 26.953 47.171 48.469 1.00 31.24 1DLC3937 ATOM 3814 NE ARG 531 27.509 46.435 49.608 1.00 37.62 1DLC3938 ATOM 3815 CZ ARG 531 26.844 45.526 50.321 1.00 41.22 1DLC3939 ATOM 3816 NH1 ARG 531 25.586 45.229 50.024 1.00 43.68 1DLC3940 ATOM 3817 NH2 ARG 531 27.438 44.914 51.342 1.00 43.63 1DLC3941 ATOM 3818 N PHE 532 31.724 50.094 49.593 1.00 19.98 1DLC3942 ATOM 3819 CA PHE 532 33.014 50.644 49.175 1.00 18.86 1DLC3943 ATOM 3820 C PHE 532 34.203 50.235 50.042 1.00 18.66 1DLC3944 ATOM 3821 O PHE 532 35.295 50.766 49.876 1.00 22.14 1DLC3945 ATOM 3822 CB PHE 532 32.947 52.174 49.060 1.00 16.92 1DLC3946 ATOM 3823 CG PHE 532 32.563 52.873 50.338 1.00 19.17 1DLC3947 ATOM 3824 CD1 PHE 532 33.496 53.066 51.356 1.00 18.16 1DLC3948 ATOM 3825 CD2 PHE 532 31.264 53.337 50.527 1.00 15.07 1DLC3949 ATOM 3826 CE1 PHE 532 33.135 53.708 52.546 1.00 17.02 1DLC3950 ATOM 3827 CE2 PHE 532 30.898 53.977 51.708 1.00 10.86 1DLC3951 ATOM 3828 CZ PHE 532 31.831 54.163 52.719 1.00 15.12 1DLC3952 ATOM 3829 N THR 533 33.998 49.284 50.951 1.00 17.51 1DLC3953 ATOM 3830 CA THR 533 35.072 48.827 51.839 1.00 14.72 1DLC3954 ATOM 3831 C THR 533 35.651 47.437 51.531 1.00 14.62 1DLC3955 ATOM 3832 O THR 533 36.485 46.945 52.279 1.00 16.18 1DLC3956 ATOM 3833 CB THR 533 34.629 48.834 53.316 1.00 13.10 1DLC3957 ATOM 3834 OG1 THR 533 33.574 47.884 53.498 1.00 17.35 1DLC3958 ATOM 3835 CG2 THR 533 34.140 50.210 53.730 1.00 9.08 1DLC3959 ATOM 3836 N GLY 534 35.193 46.797 50.457 1.00 13.58 1DLC3960 ATOM 3837 CA GLY 534 35.702 45.480 50.099 1.00 11.66 1DLC3961 ATOM 3838 C GLY 534 35.064 44.293 50.796 1.00 11.74 1DLC3962 ATOM 3839 O GLY 534 35.328 43.138 50.450 1.00 10.96 1DLC3963 ATOM 3840 N GLY 535 34.217 44.586 51.776 1.00 14.26 1DLC3964 ATOM 3841 CA GLY 535 33.524 43.554 52.528 1.00 14.95 1DLC3965 ATOM 3842 C GLY 535 32.530 44.107 53.542 1.00 16.62 1DLC3966 ATOM 3843 O GLY 535 32.129 45.269 53.460 1.00 15.43 1DLC3967 ATOM 3844 N ASP 536 32.131 43.283 54.503 1.00 15.04 1DLC3968 ATOM 3845 CA ASP 536 31.180 43.722 55.514 1.00 16.74 1DLC3969 ATOM 3846 C ASP 536 31.844 44.387 56.715 1.00 16.82 1DLC3970 ATOM 3847 O ASP 536 33.066 44.423 56.806 1.00 18.08 1DLC3971 ATOM 3848 CB ASP 536 30.265 42.566 55.935 1.00 15.87 1DLC3972 ATOM 3849 CG ASP 536 29.333 42.124 54.811 1.00 19.56 1DLC3973 ATOM 3850 OD1 ASP 536 28.899 42.978 54.003 1.00 19.60 1DLC3974 ATOM 3851 OD2 ASP 536 29.036 40.916 54.724 1.00 21.83 1DLC3975 ATOM 3852 N ILE 537 31.037 44.932 57.621 1.00 15.79 1DLC3976 ATOM 3853 CA ILE 537 31.561 45.626 58.791 1.00 15.94 1DLC3977 ATOM 3854 C ILE 537 30.911 45.174 60.094 1.00 19.56 1DLC3978 ATOM 3855 O ILE 537 29.945 44.411 60.080 1.00 21.80 1DLC3979 ATOM 3856 CB ILE 537 31.392 47.160 58.659 1.00 17.46 1DLC3980 ATOM 3857 CG1 ILE 537 29.902 47.537 58.605 1.00 18.41 1DLC3981 ATOM 3858 CG2 ILE 537 32.155 47.668 57.436 1.00 16.62 1DLC3982 ATOM 3859 CD1 ILE 537 29.628 49.004 58.312 1.00 13.27 1DLC3983 ATOM 3860 N ILE 538 31.464 45.619 61.219 1.00 19.15 1DLC3984 ATOM 3861 CA ILE 538 30.929 45.263 62.533 1.00 19.28 1DLC3985 ATOM 3862 C ILE 538 30.189 46.433 63.167 1.00 17.76 1DLC3986 ATOM 3863 O ILE 538 30.687 47.556 63.207 1.00 17.93 1DLC3987 ATOM 3864 CB ILE 538 32.047 44.748 63.506 1.00 20.58 1DLC3988 ATOM 3865 CG1 ILE 538 32.256 43.235 63.328 1.00 21.11 1DLC3989 ATOM 3866 CG2 ILE 538 31.696 45.055 64.977 1.00 15.08 1DLC3990 ATOM 3867 CD1 ILE 538 32.758 42.812 61.968 1.00 22.07 1DLC3991 ATOM 3868 N GLN 539 28.978 46.154 63.626 1.00 19.91 1DLC3992 ATOM 3869 CA GLN 539 28.139 47.142 64.283 1.00 21.14 1DLC3993 ATOM 3870 C GLN 539 28.148 46.929 65.790 1.00 21.70 1DLC3994 ATOM 3871 O GLN 539 27.816 45.847 66.273 1.00 23.99 1DLC3995 ATOM 3872 CB GLN 539 26.707 47.021 63.780 1.00 25.95 1DLC3996 ATOM 3873 CG GLN 539 25.764 48.075 64.333 1.00 30.75 1DLC3997 ATOM 3874 CD GLN 539 24.328 47.810 63.941 1.00 32.55 1DLC3998 ATOM 3875 OE1 GLN 539 23.816 48.378 62.980 1.00 33.12 1DLC3999 ATOM 3876 NE2 GLN 539 23.679 46.918 64.669 1.00 34.27 1DLC4000 ATOM 3877 N CYS 540 28.528 47.968 66.523 1.00 23.44 1DLC4001 ATOM 3878 CA CYS 540 28.564 47.939 67.983 1.00 23.84 1DLC4002 ATOM 3879 C CYS 540 27.459 48.828 68.526 1.00 24.50 1DLC4003 ATOM 3880 O CYS 540 27.331 49.985 68.133 1.00 26.64 1DLC4004 ATOM 3881 CB CYS 540 29.921 48.408 68.505 1.00 20.82 1DLC4005 ATOM 3882 SG CYS 540 31.256 47.385 67.896 1.00 24.17 1DLC4006 ATOM 3883 N THR 541 26.640 48.270 69.405 1.00 27.07 1DLC4007 ATOM 3884 CA THR 541 25.528 49.019 69.980 1.00 28.11 1DLC4008 ATOM 3885 C THR 541 25.593 49.152 71.501 1.00 29.79 1DLC4009 ATOM 3886 O THR 541 24.819 49.901 72.088 1.00 34.10 1DLC4010 ATOM 3887 CB THR 541 24.165 48.396 69.587 1.00 26.24 1DLC4011 ATOM 3888 OG1 THR 541 24.060 47.068 70.118 1.00 30.21 1DLC4012 ATOM 3889 CG2 THR 541 24.022 48.337 68.079 1.00 23.34 1DLC4013 ATOM 3890 N GLU 542 26.532 48.459 72.140 1.00 30.44 1DLC4014 ATOM 3891 CA GLU 542 26.654 48.529 73.595 1.00 29.89 1DLC4015 ATOM 3892 C GLU 542 28.070 48.788 74.082 1.00 29.72 1DLC4016 ATOM 3893 O GLU 542 29.038 48.531 73.371 1.00 28.80 1DLC4017 ATOM 3894 CB GLU 542 26.137 47.246 74.230 1.00 34.31 1DLC4018 ATOM 3895 CG GLU 542 24.633 47.084 74.162 1.00 44.89 1DLC4019 ATOM 3896 CD GLU 542 24.195 45.678 74.502 1.00 51.23 1DLC4020 ATOM 3897 OE1 GLU 542 24.867 45.025 75.332 1.00 56.34 1DLC4021 ATOM 3898 OE2 GLU 542 23.181 45.218 73.930 1.00 58.74 1DLC4022 ATOM 3899 N ASN 543 28.180 49.306 75.299 1.00 30.82 1DLC4023 ATOM 3900 CA ASN 543 29.479 49.589 75.894 1.00 33.54 1DLC4024 ATOM 3901 C ASN 543 30.123 48.319 76.434 1.00 35.03 1DLC4025 ATOM 3902 O ASN 543 29.534 47.626 77.254 1.00 40.96 1DLC4026 ATOM 3903 CB ASN 543 29.338 50.595 77.028 1.00 33.74 1DLC4027 ATOM 3904 CG ASN 543 29.091 51.994 76.531 1.00 35.64 1DLC4028 ATOM 3905 OD1 ASN 543 29.652 52.412 75.527 1.00 37.08 1DLC4029 ATOM 3906 ND2 ASN 543 28.267 52.739 77.245 1.00 39.76 1DLC4030 ATOM 3907 N GLY 544 31.326 48.016 75.969 1.00 33.62 1DLC4031 ATOM 3908 CA GLY 544 32.029 46.833 76.426 1.00 33.21 1DLC4032 ATOM 3909 C GLY 544 32.845 46.227 75.309 1.00 34.24 1DLC4033 ATOM 3910 O GLY 544 33.154 46.903 74.328 1.00 34.87 1DLC4034 ATOM 3911 N SER 545 33.226 44.964 75.454 1.00 34.84 1DLC4035 ATOM 3912 CA SER 545 33.997 44.305 74.402 1.00 37.03 1DLC4036 ATOM 3913 C SER 545 33.183 44.282 73.118 1.00 35.99 1DLC4037 ATOM 3914 O SER 545 31.978 44.513 73.126 1.00 39.41 1DLC4038 ATOM 3915 CB SER 545 34.370 42.873 74.785 1.00 39.43 1DLC4039 ATOM 3916 OG SER 545 35.464 42.856 75.677 1.00 47.60 1DLC4040 ATOM 3917 N ALA 546 33.835 43.972 72.015 1.00 31.02 1DLC4041 ATOM 3918 CA ALA 546 33.133 43.941 70.757 1.00 27.54 1DLC4042 ATOM 3919 C ALA 546 33.600 42.772 69.929 1.00 26.24 1DLC4043 ATOM 3920 O ALA 546 32.809 41.914 69.551 1.00 27.56 1DLC4044 ATOM 3921 CB ALA 546 33.356 45.248 70.012 1.00 28.49 1DLC4045 ATOM 3922 N ALA 547 34.905 42.705 69.705 1.00 24.78 1DLC4046 ATOM 3923 CA ALA 547 35.471 41.643 68.894 1.00 24.38 1DLC4047 ATOM 3924 C ALA 547 36.864 41.231 69.329 1.00 25.97 1DLC4048 ATOM 3925 O ALA 547 37.629 42.033 69.874 1.00 26.00 1DLC4049 ATOM 3926 CB ALA 547 35.494 42.068 67.427 1.00 19.70 1DLC4050 ATOM 3927 N THR 548 37.163 39.955 69.114 1.00 27.03 1DLC4051 ATOM 3928 CA THR 548 38.467 39.387 69.419 1.00 24.71 1DLC4052 ATOM 3929 C THR 548 38.967 38.779 68.118 1.00 24.86 1DLC4053 ATOM 3930 O THR 548 38.313 37.924 67.516 1.00 26.12 1DLC4054 ATOM 3931 CB THR 548 38.401 38.296 70.501 1.00 24.53 1DLC4055 ATOM 3932 OG1 THR 548 37.845 38.849 71.699 1.00 26.86 1DLC4056 ATOM 3933 CG2 THR 548 39.805 37.768 70.805 1.00 23.92 1DLC4057 ATOM 3934 N ILE 549 40.090 39.293 67.651 1.00 24.94 1DLC4058 ATOM 3935 CA ILE 549 40.694 38.836 66.418 1.00 24.02 1DLC4b59 ATOM 3936 C ILE 549 42.085 38.263 66.693 1.00 23.26 1DLC4060 ATOM 3937 O ILE 549 42.839 38.798 67.503 1.00 21.17 1DLC4061 ATOM 3938 CB ILE 549 40.730 39.992 65.387 1.00 25.33 1DLC4062 ATOM 3939 CG1 ILE 549 41.441 39.562 64.104 1.00 26.33 1DLC4063 ATOM 3940 CG2 ILE 549 41.342 41.241 66.004 1.00 27.68 1DLC4064 ATOM 3941 CD1 ILE 549 41.136 40.472 62.934 1.00 28.86 1DLC4065 ATOM 3942 N TYR 550 42.375 37.116 66.089 1.00 24.17 1DLC4066 ATOM 3943 CA TYR 550 43.661 36.461 66.272 1.00 24.37 1DLC4067 ATOM 3944 C TYR 550 44.674 37.003 65.272 1.00 26.11 1DLC4068 ATOM 3945 O TYR 550 44.429 37.047 64.065 1.00 29.47 1DLC4069 ATOM 3946 CB TYR 550 43.522 34.949 66.131 1.00 25.12 1DLC4070 ATOM 3947 CG TYR 550 44.776 34.184 66.470 1.00 24.27 1DLC4071 ATOM 3948 CD1 TYR 550 45.802 34.041 65.533 1.00 26.12 1DLC4072 ATOM 3949 CD2 TYR 550 44.932 33.590 67.721 1.00 23.82 1DLC4073 ATOM 3950 CE1 TYR 550 46.944 33.327 65.827 1.00 22.97 1DLC4074 ATOM 3951 CE2 TYR 550 46.075 32.669 68.025 1.00 22.49 1DLC4075 ATOM 3952 CZ TYR 550 47.071 32.743 67.073 1.00 23.77 1DLC4076 ATOM 3953 OH TYR 550 48.194 32.015 67.361 1.00 31.16 1DLC4077 ATOM 3954 N VAL 551 45.836 37.362 65.791 1.00 24.14 1DLC4078 ATOM 3955 CA VAL 551 46.893 37.947 64.995 1.00 24.15 1DLC4079 ATOM 3956 C VAL 551 48.182 37.117 64.962 1.00 23.16 1DLC4080 ATOM 3957 O VAL 551 48.576 36.522 65.962 1.00 23.67 1DLC4081 ATOM 3958 CB VAL 551 47.132 39.393 65.500 1.00 21.76 1DLC4082 ATOM 3959 CG1 VAL 551 48.555 39.817 65.337 1.00 27.10 1DLC4083 ATOM 3960 CG2 VAL 551 46.210 40.334 64.761 1.00 23.25 1DLC4084 ATOM 3961 N THR 552 48.810 37.065 63.792 1.00 23.48 1DLC4085 ATOM 3962 CA THR 552 50.057 36.324 63.597 1.00 24.21 1DLC4086 ATOM 3963 C THR 552 51.219 37.238 63.229 1.00 24.68 1DLC4087 ATOM 3964 O THR 552 51.314 37.698 62.096 1.00 25.97 1DLC4088 ATOM 3965 CB THR 552 49.928 35.277 62.471 1.00 23.38 1DLC4089 ATOM 3966 OG1 THR 552 48.951 34.300 62.838 1.00 29.47 1DLC4090 ATOM 3967 CG2 THR 552 51.251 34.579 62.225 1.00 23.28 1DLC4091 ATOM 3968 N PRO 553 52.096 37.548 64.193 1.00 30.06 1DLC4092 ATOM 3969 CA PRO 553 53.254 38.416 63.925 1.00 31.84 1DLC4093 ATOM 3970 C PRO 553 54.218 37.699 62.977 1.00 33.44 1DLC4094 ATOM 3971 O PRO 553 54.444 36.497 63.123 1.00 32.03 1DLC4095 ATOM 3972 CB PRO 553 53.591 38.591 65.313 1.00 32.97 1DLC4096 ATOM 3973 CG PRO 553 52.671 38.468 66.241 1.00 33.91 1DLC4097 ATOM 3974 CD PRO 553 51.962 37.281 65.637 1.00 32.11 1DLC4098 ATOM 3975 N ASP 554 54.758 38.413 61.993 1.00 35.95 1DLC4099 ATOM 3976 CA ASP 554 55.676 37.788 61.036 1.00 41.00 1DLC4100 ATOM 3977 C ASP 554 57.150 37.717 61.467 1.00 42.22 1DLC4101 ATOM 3978 O ASP 554 57.949 37.037 60.829 1.00 46.36 1DLC4102 ATOM 3979 CB ASP 554 55.570 38.457 59.660 1.00 43.46 1DLC4103 ATOM 3980 CG ASP 554 56.373 39.740 59.569 1.00 46.10 1DLC4104 ATOM 3981 OD1 ASP 554 56.390 40.500 60.563 1.00 50.84 1DLC4105 ATOM 3982 OD2 ASP 554 56.992 39.985 58.509 1.00 45.05 1DLC4106 ATOM 3983 N VAL 555 57.524 38.457 62.506 1.00 42.99 1DLC4107 ATOM 3984 CA VAL 555 58.904 38.429 62.991 1.00 41.56 1DLC4108 ATOM 3985 C VAL 555 58.988 39.030 64.454 1.00 45.35 1DLC4109 ATOM 3986 O VAL 555 58.022 38.149 65.208 1.00 46.82 1DLC4110 ATOM 3987 CB VAL 555 59.634 39.778 62.809 1.00 36.93 1DLC4111 ATOM 3988 CG1 VAL 555 59.739 40.121 61.345 1.00 36.03 1DLC4112 ATOM 3989 CG2 VAL 555 58.936 40.878 63.583 1.00 32.39 1DLC4113 ATOM 3990 N SER 556 60.174 37.591 64.854 1.00 48.53 1DLC4114 ATOM 3991 CA SER 556 60.434 37.149 66.224 1.00 48.94 1DLC4115 ATOM 3992 C SER 556 60.820 38.260 67.211 1.00 46.00 1DLC4116 ATOM 3993 O SER 556 60.361 38.265 68.359 1.00 48.54 1DLC4117 ATOM 3994 CB SER 556 61.524 36.079 66.189 1.00 52.10 1DLC4118 ATOM 3995 OG SER 556 62.482 36.395 65.177 1.00 57.59 1DLC4119 ATOM 3996 N TYR 557 61.669 39.188 66.769 1.00 40.86 1DLC4120 ATOM 3997 CA TYR 557 62.129 40.295 67.614 1.00 35.42 1DLC4121 ATOM 3998 C TYR 557 61.042 41.301 67.985 1.00 34.52 1DLC4122 ATOM 3999 O TYR 557 60.016 41.395 67.316 1.00 35.21 1DLC4123 ATOM 4000 CB TYR 557 63.295 41.021 66.956 1.00 30.14 1DLC4124 ATOM 4001 CG TYR 557 62.963 41.630 65.615 1.00 27.40 1DLC4125 ATOM 4002 CD1 TYR 557 62.352 42.886 65.627 1.00 25.94 1DLC4126 ATOM 4003 CD2 TYR 557 63.288 40.971 64.436 1.00 20.52 1DLC4127 ATOM 4004 CE1 TYR 557 62.078 43.464 64.301 1.00 24.25 1DLC4128 ATOM 4005 CE2 TYR 557 63.019 41.542 63.204 1.00 24.51 1DLC4129 ATOM 4006 CZ TYR 557 62.414 42.787 63.138 1.00 26.31 1DLC4130 ATOM 4007 OH TYR 557 62.135 43.344 61.904 1.00 29.41 1DLC4131 ATOM 4008 N SER 558 61.331 42.118 68.991 1.00 33.34 1DLC4132 ATOM 4009 CA SER 558 60.395 43.114 69.512 1.00 32.79 1DLC4133 ATOM 4010 C SER 558 60.019 44.336 68.656 1.00 31.63 1DLC4134 ATOM 4011 O SER 558 60.148 45.481 69.098 1.00 30.68 1DLC4135 ATOM 4012 CB SER 558 60.855 43.563 70.904 1.00 35.65 1DLC4136 ATOM 4013 OG SER 558 62.262 43.758 70.943 1.00 41.15 1DLC4137 ATOM 4014 N GLN 559 59.524 44.085 67.447 1.00 30.48 1DLC4138 ATOM 4015 CA GLN 559 59.077 45.140 66.533 1.00 29.46 1DLC4139 ATOM 4016 C GLN 559 57.911 45.942 67.143 1.00 31.04 1DLC4140 ATOM 4017 O GLN 559 56.986 45.378 67.738 1.00 26.59 1DLC4141 ATOM 4018 CB GLN 559 58.618 44.519 65.213 1.00 30.68 1DLC4142 ATOM 4019 CG GLN 559 57.983 45.485 64.227 1.00 30.37 1DLC4143 ATOM 4020 CD GLN 559 58.987 46.419 63.591 1.00 30.94 1DLC4144 ATOM 4021 OE1 GLN 559 58.686 47.634 63.689 1.00 33.08 1DLC4145 ATOM 4022 NE2 GLN 559 59.984 45.854 62.933 1.00 32.16 1DLC4146 ATOM 4023 N LYS 560 57.983 47.262 67.003 1.00 32.69 1DLC4147 ATOM 4024 CA LYS 560 56.959 48.156 67.521 1.00 32.07 1DLC4148 ATOM 4025 C LYS 560 56.011 46.599 66.419 1.00 28.30 1DLC4149 ATOM 4026 O LYS 560 56.401 48.725 65.256 1.00 23.65 1DLC4150 ATOM 4027 CB LYS 560 57.593 49.380 68.186 1.00 37.57 1DLC4151 ATOM 4028 CG LYS 560 58.226 49.100 69.538 1.00 44.56 1DLC4152 ATOM 4029 CD LYS 560 59.281 50.154 69.855 1.00 55.46 1DLC4153 ATOM 4030 CE LYS 560 58.671 51.528 70.103 1.00 59.12 1DLC4154 ATOM 4031 NZ LYS 560 58.034 51.582 71.456 1.00 66.07 1DLC4155 ATOM 4032 N TYR 561 54.762 48.833 66.816 1.00 28.00 1DLC4156 ATOM 4033 CA TYR 561 53.694 49.255 65.919 1.00 24.77 1DLC4157 ATOM 4034 C TYR 561 52.816 50.369 66.469 1.00 24.89 1DLC4158 ATOM 4035 O TYR 561 52.771 50.628 67.675 1.00 25.20 1DLC4159 ATOM 4036 CB TYR 561 52.768 48.073 65.623 1.00 22.54 1DLC4160 ATOM 4037 CG TYR 561 53.442 46.903 64.956 1.00 21.90 1DLC4161 ATOM 4038 CD1 TYR 561 54.015 45.881 65.714 1.00 19.30 1DLC4162 ATOM 4039 CD2 TYR 561 53.500 46.812 63.566 1.00 15.01 1DLC4163 ATOM 4040 CE1 TYR 561 54.627 44.801 65.103 1.00 19.55 1DLC4164 ATOM 4041 CE2 TYR 561 54.109 45.742 62.950 1.00 16.21 1DLC4165 ATOM 4042 CZ TYR 561 54.666 44.736 63.722 1.00 20.28 1DLC4166 ATOM 4043 OH TYR 561 55.240 43.642 63.107 1.00 33.74 1DLC416T ATOM 4044 N ARG 562 52.153 51.C50 65.544 1.00 25.77 1DLC4168 ATOM 4045 CA ARG 562 51.179 52.094 65.854 1.00 23.64 1DLC4169 ATOM 4046 C ARG 562 49.907 51.506 65.251 1.00 23.48 1DLC4170 ATOM 4047 O ARG 562 49.960 50.823 64.216 1.00 20.35 1DLC4171 ATOM 4048 CB ARG 562 51.484 53.414 65.132 1.00 22.03 1DLC4172 ATOM 4049 CG ARG 562 52.666 54.190 65.655 1.00 30.26 1DLC4173 ATOM 4050 CD ARG 562 52.432 54.744 67.051 1.00 32.80 1DLC4174 ATOM 4051 NE ARG 562 51.345 55.719 67.109 1.00 39.02 1DLC4175 ATOM 4052 CZ ARG 562 51.269 56.825 66.372 1.00 40.34 1DLC4176 ATOM 4053 NH1 ARG 562 52.217 57.124 65.494 1.00 42.09 1DLC4177 ATOM 4054 NH2 ARG 562 50.237 57.645 66.521 1.00 42.48 1DLC4178 ATOM 4055 N ALA 563 48.773 51.741 65.894 1.00 22.02 1DLC4179 ATOM 4056 CA ALA 563 47.515 51.235 65.378 1.00 18.79 1DLC4180 ATOM 4057 C ALA 563 46.629 52.386 64.933 1.00 18.02 1DLC4181 ATOM 4058 O ALA 563 46.640 53.461 65.525 1.00 20.34 1DLC4182 ATOM 4059 CB ALA 563 46.800 50.392 66.440 1.00 18.24 1DLC4183 ATOM 4060 N ARG 564 45.908 52.159 63.846 1.00 18.32 1DLC4184 ATOM 4061 CA ARG 564 44.960 53.118 63.290 1.00 16.43 1DLC4185 ATOM 4062 C ARG 564 43.631 52.379 63.170 1.00 18.85 1DLC4186 ATOM 4063 O ARG 564 43.602 51.185 62.858 1.00 17.80 1DLC4187 ATOM 4064 CB ARG 564 45.338 53.481 61.874 1.00 15.45 1DLC4188 ATOM 4065 CG ARG 564 46.236 54.635 61.654 1.00 14.12 1DLC4189 ATOM 4066 CD ARG 564 46.452 54.611 60.165 1.00 18.52 1DLC4190 ATOM 4067 NE ARG 564 47.230 55.713 59.648 1.00 20.74 1DLC4191 ATOM 4068 CZ ARG 564 47.640 55.791 58.390 1.00 18.32 1DLC4192 ATOM 4069 NH1 ARG 564 47.359 54.825 57.523 1.00 13.13 1DLC4193 ATOM 4070 NH2 ARG 564 48.288 56.872 57.998 1.00 26.68 1DLC4194 ATOM 4071 N ILE 565 42.527 53.092 63.319 1.00 18.95 1DLC4195 ATOM 4072 CA ILE 565 41.238 52.440 63.187 1.00 17.58 1DLC4196 ATOM 4073 C ILE 565 40.301 53.192 62.229 1.00 19.97 1DLC4197 ATOM 4074 O ILE 565 40.261 54.430 62.223 1.00 20.07 1DLC4198 ATOM 4075 CB ILE 565 40.612 52.176 64.579 1.00 14.60 1DLC4199 ATOM 4076 CG1 ILE 565 39.335 51.353 64.448 1.00 16.02 1DLC4200 ATOM 4077 CG2 ILE 565 40.402 53.475 65.331 1.00 15.20 1DLC4201 ATOM 4078 CD1 ILE 565 38.980 50.629 65.727 1.00 16.53 1DLC4202 ATOM 4079 N HIS 566 39.695 52.438 61.307 1.00 18.25 1DLC4203 ATOM 4080 CA HIS 566 38.752 52.981 60.329 1.00 14.18 1DLC4204 ATOM 4081 C HIS 566 37.366 52.640 60.859 1.00 15.68 1DLC4205 ATOM 4082 O HIS 566 36.950 51.482 60.816 1.00 16.47 1DLC4206 ATOM 4083 CB HIS 566 38.960 52.341 58.958 1.00 11.65 1DLC4207 ATOM 4084 CG HIS 566 38.314 53.093 57.831 1.00 11.11 1DLC4208 ATOM 4085 ND1 HIS 566 37.635 52.465 56.808 1.00 11.16 1DLC4209 ATOM 4086 CD2 HIS 566 38.258 54.418 57.558 1.00 11.95 1DLC4210 ATOM 4087 CE1 HIS 566 37.191 53.366 55.951 1.00 8.58 1DLC4211 ATOM 4088 NE2 HIS 566 37.554 54.561 56.383 1.00 13.33 1DLC4212 ATOM 4089 N TYR 567 36.654 53.654 61.339 1.00 16.40 1DLC4213 ATOM 4090 CA TYR 567 35.326 53.471 61.935 1.00 17.25 1DLC4214 ATOM 4091 C TYR 567 34.356 54.630 61.612 1.00 17.40 1DLC4215 ATOM 4092 O TYR 567 34.730 55.628 60.982 1.00 17.78 1DLC4216 ATOM 4093 CB TYR 567 35.485 53.406 63.471 1.00 13.75 1DLC4217 ATOM 4094 CG TYR 567 35.831 54.771 64.026 1.00 17.11 1DLC4218 ATOM 4095 CD1 TYR 567 37.075 55.356 63.767 1.00 16.44 1DLC4219 ATOM 4096 CD2 TYR 567 34.866 55.549 64.674 1.00 18.59 1DLC4220 ATOM 4097 E1 TYR 567 37.341 56.675 64.121 1.00 14.77 1DLC4221 ATOM 4098 CE2 TYR 567 35.129 56.872 65.033 1.00 14.24 1DLC4222 ATOM 4099 CZ TYR 567 36.365 57.423 64.751 1.00 12.88 1DLC4223 ATOM 4100 OH TYR 567 36.624 58.727 65.094 1.00 18.70 1DLC4224 ATOM 4101 N ALA 568 33.128 54.491 62.114 1.00 15.14 1DLC4225 ATOM 4102 CA ALA 568 32.062 55.486 61.997 1.00 11.71 1DLC4226 ATOM 4103 C ALA 568 31.335 55.432 63.347 1.00 13.73 1DLC4227 ATOM 4104 O ALA 568 31.115 54.349 63.895 1.00 14.98 1DLC4228 ATOM 4105 CB ALA 568 31.119 55.140 60.872 1.00 8.00 1DLC4229 ATOM 4106 N SER 569 31.010 56.588 63.913 1.00 12.74 1DLC4230 ATOM 4107 CA SER 569 30.344 56.623 65.209 1.00 13.22 1DLC4231 ATOM 4108 C SER 569 29.342 57.768 65.333 1.00 19.84 1DLC4232 ATOM 4109 O SER 569 29.544 58.847 64.767 1.00 23.01 1DLC4233 ATOM 4110 CB SER 569 31.384 56.751 66.322 1.00 10.39 1DLC4234 ATOM 4111 OG SER 569 30.781 56.784 67.602 1.00 12.68 1DLC4235 ATOM 4112 N THR 570 28.262 57.530 66.075 1.00 20.82 1DLC4236 ATOM 4113 CA THR 570 27.246 58.561 66.302 1.00 22.66 1DLC4237 ATOM 4114 C THR 570 27.608 59.465 67.494 1.00 24.67 1DLC4238 ATOM 4115 O THR 570 26.978 60.496 67.720 1.00 26.92 1DLC4239 ATOM 4116 CB THR 570 25.842 57.957 66.517 1.00 19.64 1DLC4240 ATOM 4117 OG1 THR 570 25.870 57.024 67.602 1.00 17.72 1DLC4241 ATOM 4118 CG2 THR 570 25.384 57.248 65.262 1.00 18.85 1DLC4242 ATOM 4119 N SER 571 28.646 59.085 68.237 1.00 26.33 1DLC4243 ATOM 4120 CA SER 571 29.107 59.869 69.386 1.00 26.65 1DLC4244 ATOM 4121 C SER 571 30.614 59.783 69.597 1.00 27.37 1DLC4245 ATOM 4122 O SER 571 31.309 59.001 68.942 1.00 26.89 1DLC4246 ATOM 4123 CB SER 571 28.437 59.388 70.677 1.00 28.07 1DLC4247 ATOM 4124 OG SER 571 29.047 58.203 71.173 1.00 26.73 1DLC4248 ATOM 4125 N GLN 572 31.113 60.621 70.502 1.00 29.31 1DLC4249 ATOM 4126 CA GLN 572 32.520 60.596 70.871 1.00 27.70 1DLC4250 ATOM 4127 C GLN 572 32.645 59.287 71.648 1.00 25.42 1DLC4251 ATOM 4128 O GLN 572 31.771 58.935 72.444 1.00 25.29 1DLC4252 ATOM 4129 CB GLN 572 32.891 61.789 71.763 1.00 31.54 1DLC4253 ATOM 4130 CG GLN 572 32.791 63.161 71.076 1.00 40.28 1DLC4254 ATOM 4131 CD GLN 572 33.796 64.189 71.616 1.00 45.09 1DLC4255 ATOM 4132 OE1 GLN 572 34.886 64.347 71.064 1.00 49.93 1DLC4256 ATOM 4133 NE2 GLN 572 33.428 64.892 72.685 1.00 44.38 1DLC4257 ATOM 4134 N ILE 573 33.702 58.543 71.379 1.00 25.62 1DLC4258 ATOM 4135 CA ILE 573 33.891 57.252 72.027 1.00 24.87 1DLC4259 ATOM 4136 C ILE 573 35.318 56.964 72.451 1.00 23.49 1DLC4260 ATOM 4137 O ILE 573 36.244 57.724 72.165 1.00 24.22 1DLC4261 ATOM 4138 CB ILE 573 33.472 56.120 71.084 1.00 24.02 1DLC4262 ATOM 4139 CG1 ILE 573 34.175 56.308 69.731 1.00 20.45 1DLC4263 ATOM 4140 CG2 ILE 573 31.954 56.080 70.962 1.00 23.19 1DLC4264 ATOM 4141 CD1 ILE 573 33.929 55.210 68.750 1.00 21.25 1DLC4265 ATOM 4142 N THR 574 35.477 55.856 73.156 1.00 21.66 1DLC4266 ATOM 4143 CA THR 574 36.786 55.424 73.591 1.00 19.94 1DLC4267 ATOM 4144 C THR 574 36.991 54.009 73.106 1.00 21.16 1DLC4268 ATOM 4145 O THR 574 36.142 53.140 73.300 1.00 20.88 1DLC4269 ATOM 4146 CB THR 574 36.936 55.453 75.123 1.00 21.34 1DLC4270 ATOM 4147 OG1 THR 574 36.902 56.808 75.579 1.00 27.16 1DLC4271 ATOM 4148 CG2 THR 574 38.251 54.835 75.549 1.00 18.62 1DLC4272 ATOM 4149 N PHE 575 38.085 53.806 72.392 1.00 21.90 1DLC4273 ATOM 4150 CA PHE 575 38.433 52.488 71.904 1.00 21.69 1DLC4274 ATOM 4151 C PHE 575 39.556 51.976 72.801 1.00 22.38 1DLC4275 ATOM 4152 O PHE 575 40.441 52.741 73.185 1.00 24.96 1DLC4276 ATOM 4153 CB PHE 575 38.904 52.557 70.447 1.00 22.02 1DLC4277 ATOM 4154 CG PHE 575 37.782 52.563 69.433 1.00 22.92 1DLC4278 ATOM 4155 CD1 PHE 575 36.741 51.637 69.514 1.00 23.97 1DLC4279 ATOM 4156 CD2 PHE 575 37.792 53.462 68.370 1.00 22.78 1DLC4280 ATOM 4157 CE1 PHE 575 35.729 51.604 68.550 1.00 23.30 1DLC4281 ATOM 4158 CE2 PHE 575 36.785 53.438 67.402 1.00 24.47 1DLC4282 ATOM 4159 CZ PHE 575 35.751 52.502 67.495 1.00 22.95 1DLC4283 ATOM 4160 N THR 576 39.470 50.715 73.208 1.00 22.42 1DLC4284 ATOM 4161 CA THR 576 40.508 50.112 74.046 1.00 23.02 1DLC4285 ATOM 4162 C THR 576 41.004 48.841 73.362 1.00 26.73 1DLC4286 ATOM 4163 O THR 576 40.217 48.083 72.775 1.00 27.65 1DLC4287 ATOM 4164 CB THR 576 40.005 49.761 75.472 1.00 22.77 1DLC4288 ATOM 4165 OG1 THR 576 39.490 50.938 76.107 1.00 22.85 1DLC4289 ATOM 4166 CG2 THR 576 41.151 49.218 76.329 1.00 20.19 1DLC4290 ATOM 4167 N LEU 577 42.322 48.661 73.364 1.00 26.31 1DLC4291 ATOM 4168 CA LEU 577 42.952 47.491 72.762 1.00 23.97 1DLC4292 ATOM 4169 C LEU 577 43.588 46.622 73.834 1.00 22.18 1DLq4293 ATOM 4170 O LEU 577 44.242 47.119 74.752 1.00 22.92 1DLC4294 ATOM 4171 CB LEU 577 44.018 47.900 71.744 1.00 21.75 1DLC4295 ATOM 4172 CG LEU 577 43.586 48.805 70.592 1.00 22.22 1DLC4296 ATOM 4173 CD1 LEU 577 44.732 49.008 69.614 1.00 20.22 1DLC4297 ATOM 4174 CD2 LEU 577 42.401 48.193 69.894 1.00 22.18 1DLC4298 ATOM 4175 N SER 578 43.367 45.321 73.721 1.00 22.27 1DLC4299 ATOM 4176 CA SER 578 43.926 44.365 74.660 1.00 22.35 1DLC4300 ATOM 4177 C SER 578 44.578 43.224 73.907 1.00 23.31 1DLC4301 ATOM 4178 O SER 578 44.143 42.859 72.814 1.00 23.83 1DLC4302 ATOM 4179 CB SER 578 42.839 43.784 75.564 1.00 21.54 1DLC4303 ATOM 4180 OG SER 578 42.197 44.801 76.303 1.00 25.56 1DLC4304 ATOM 4181 N LEU 579 45.659 42.708 74.475 1.00 23.36 1DLC4305 ATOM 4182 CA LEU 579 46.371 41.573 73.910 1.00 23.41 1DLC4306 ATOM 4183 C LEU 579 46.271 40.490 74.968 1.00 23.47 1DLC4307 ATOM 4184 O LEU 579 46.635 40.709 76.124 1.00 21.83 1DLC4308 ATOM 4185 CB LEU 579 47.836 41.907 73.655 1.00 25.86 1DLC4309 ATOM 4186 CG LEU 579 48.258 42.090 72.203 1.00 30.80 1DLC4310 ATOM 4187 CD1 LEU 579 49.782 42.146 72.138 1.00 31.83 1DLC4311 ATOM 4188 CD2 LEU 579 47.730 40.932 71.362 1.00 31.68 1DLC4312 ATOM 4189 N ASP 580 45.694 39.357 74.592 1.00 23.35 1DLC4313 ATOM 4190 CA ASP 580 45.514 38.243 75.512 1.00 22.65 1DLC4314 ATOM 4191 C ASP 580 44.902 38.664 76.853 1.00 21.10 1DLC4315 ATOM 4192 O ASP 580 45.335 38.238 77.917 1.00 22.53 1DLC4316 ATOM 4193 CB ASP 580 46.832 37.474 75.698 1.00 26.17 1DLC4317 ATOM 4194 CG ASP 580 47.291 36.765 74.416 1.00 31.25 1DLC4318 ATOM 4195 OD1 ASP 580 46.497 36.658 73.459 1.00 33.31 1DLC4319 ATOM 4196 OD2 ASP 580 48.450 36.303 74.359 1.00 36.06 1DLC4320 ATOM 4197 N GLY 581 43.917 39.552 76.786 1.00 21.32 1DLC4321 ATOM 4198 CA GLY 581 43.227 40.002 77.981 1.00 21.27 1DLC4322 ATOM 4199 C GLY 581 43.824 41.150 78.764 1.00 22.88 1DLC4323 ATOM 4200 O GLY 581 43.290 41.536 79.805 1.00 25.91 1DLC4324 ATOM 4201 N ALA 582 44.931 41.698 78.291 1.00 23.56 1DLC4325 ATOM 4202 CA ALA 582 45.571 42.810 78.985 1.00 21.79 1DLC4326 ATOM 4203 C ALA 582 45.518 44.085 78.136 1.00 22.18 1DLC4327 ATOM 4204 O ALA 582 45.914 44.083 76.965 1.00 23.55 1DLC4328 ATOM 4205 CB ALA 582 47.005 42.451 79.323 1.00 19.42 1DLC4329 ATOM 4206 N PRO 583 44.975 45.177 78.698 1.00 21.27 1DLC4330 ATOM 4207 CA PRO 583 44.875 46.448 77.971 1.00 21.05 1DLC4331 ATOM 4208 C PRO 583 46.252 47.058 77.716 1.00 22.08 1DLC4332 ATOM 4209 O PRO 583 47.119 47.046 78.592 1.00 23.88 1DLC4333 ATOM 4210 CB PRO 583 44.089 47.344 78.939 1.00 19.25 1DLC4334 ATOM 4211 CG PRO 583 43.411 46.393 79.873 1.00 18.79 1DLC4335 ATOM 4212 CD PRO 583 44.427 45.310 80.059 1.00 20.08 1DLC4336 ATOM 4213 N PHE 584 46.462 47.585 76.522 1.00 20.46 1DLC4337 ATOM 4214 CA PHE 584 47.734 48.217 76.232 1.00 22.26 1DLC4338 ATOM 4215 C PHE 584 47.560 49.576 75.572 1.00 24.61 1DLC4339 ATOM 4216 O PHE 584 48.451 50.416 75.608 1.00 29.88 1DLC4340 ATOM 4217 CB PHE 584 48.622 47.308 75.381 1.00 17.78 1DLC4341 ATOM 4218 CG PHE 584 48.113 47.075 73.992 1.00 16.94 1DLC4342 ATOM 4219 CD1 PHE 584 48.482 47.921 72.954 1.00 15.22 1DLC4343 ATOM 4220 CD2 PHE 584 47.313 45.981 73.710 1.00 12.59 1DLC4344 ATOM 4221 CE1 PHE 584 48.067 47.678 71.666 1.00 16.40 1DLC4345 ATOM 4222 CE2 PHE 584 46.894 45.730 72.420 1.00 16.89 1DLC4346 ATOM 4223 CZ PHE 584 47.272 46.578 71.391 1.00 17.05 1DLC4347 ATOM 4224 N ASN 585 46.399 49.799 74.981 1.00 25.77 1DLC4348 ATOM 4225 CA ASN 585 46.138 51.064 74.319 1.00 27.68 1DLC4349 ATOM 4226 C ASN 585 44.688 51.488 74.531 1.00 28.54 1DLC4350 ATOM 4227 O ASN 585 43.770 50.671 74.499 1.00 30.79 1DLC4351 ATOM 4228 CB ASN 585 46.433 50.944 72.822 1.00 30.11 1DLC4352 ATOM 4229 CG ASN 585 47.358 52.038 72.310 1.00 31.24 1DLC4353 ATOM 4230 OD1 ASN 585 47.347 53.171 72.796 1.00 36.32 1DLC4354 ATOM 4231 ND2 ASN 585 48.145 51.709 71.303 1.00 34.47 1DLC4355 ATOM 4232 N GLN 586 44.494 52.764 74.812 1.00 27.87 1DLC4356 ATOM 4233 CA GLN 586 43.161 53.304 75.010 1.00 28.50 1DLC4357 ATOM 4234 C GLN 586 43.216 54.725 74.525 1.00 27.04 1DLC4358 ATOM 4235 O GLN 586 44.153 55.445 74.850 1.00 29.74 1DLC4359 ATOM 4236 CB GLN 586 42.782 53.287 76.485 1.00 29.22 1DLC4360 ATOM 4237 CG GLN 586 41.398 53.806 76.740 1.00 29.84 1DLC4361 ATOM 4238 CD GLN 586 41.013 53.713 78.189 1.00 34.57 1DLC4362 ATOM 4239 OE1 GLN 586 41.628 54.350 79.047 1.00 35.42 1DLC4363 ATOM 4240 NE2 GLN 586 40.001 52.908 78.481 1.00 35.86 1DLC4364 ATOM 4241 N TYR 587 42.239 55.131 73.730 1.00 25.37 1DLC4365 ATOM 4242 CA TYR 587 42.248 56.492 73.222 1.00 26.60 1DLC4366 ATOM 4243 C TYR 587 40.850 57.033 72.971 1.00 25.35 1DLC4367 ATOM 4244 O TYR 587 39.871 56.292 72.967 1.00 26.48 1DLC4368 ATOM 4245 CB TYR 587 43.087 56.569 71.940 1.00 24.36 1DLC4369 ATOM 4246 CG TYR 587 43.718 57.923 71.683 1.00 23.54 1DLC4370 ATOM 4247 CD1 TYR 587 44.469 58.558 72.669 1.00 26.89 1DLC4371 ATOM 4248 CD2 TYR 587 43.599 58.551 70.443 1.00 23.40 1DLC4372 ATOM 4249 CE1 TYR 587 45.093 59.781 72.427 1.00 26.78 1DLC4373 ATOM 4250 CE2 TYR 587 44.217 59.774 70.191 1.00 24.34 1DLC4374 ATOM 4251 CZ TYR 587 44.966 60.379 71.190 1.00 26.40 1DLC4375 ATOM 4252 OH TYR 587 45.616 61.567 70.954 1.00 29.54 1DLC4376 ATOM 4253 N TYR 588 40.777 58.341 72.782 1.00 26.44 1DLC4377 ATOM 4254 CA TYR 588 39.521 59.022 72.524 1.00 27.44 1DLC4378 ATOM 4255 C TYR 588 39.356 59.223 71.016 1.00 26.50 1DLC4379 ATOM 4256 O TYR 588 40.329 59.529 70.320 1.00 23.62 1DLC4380 ATOM 4257 CB TYR 588 39.524 60.372 73.218 1.00 33.96 1DLC4381 ATOM 4258 CG TYR 588 39.899 60.333 74.685 1.00 47.28 1DLC4382 ATOM 4259 CD1 TYR 588 41.220 60.098 75.091 1.00 53.44 1DLC4383 ATOM 4260 CD2 TYR 588 38.949 60.612 75.668 1.00 54.01 1DLC4384 ATOM 4261 CE1 TYR 588 41.583 60.150 76.443 1.00 58.54 1DLC4385 ATOM 4262 CE2 TYR 588 39.297 60.670 77.018 1.00 60.11 1DLC4386 ATOM 4263 CZ TYR 588 40.613 60.443 77.404 1.00 61.86 1DLC4387 ATOM 4264 OH TYR 588 40.941 60.543 78.746 1.00 65.13 1DLC4388 ATOM 4265 N PHE 589 38.132 59.026 70.518 1.00 25.50 1DLC4389 ATOM 4266 CA PHE 589 37.821 59.174 69.089 1.00 23.66 1DLC4390 ATOM 4267 C PHE 589 36.558 59.994 68.795 1.00 22.64 1DLC4391 ATOM 4268 O PHE 589 35.549 59.901 69.493 1.00 23.58 1DLC4392 ATOM 4269 CB PHE 589 37.763 57.803 68.414 1.00 22.61 1DLC4393 ATOM 4270 CG PHE 589 39.078 57.071 68.446 1.00 24.27 1DLC4394 ATOM 4271 CD1 PHE 589 39.422 56.279 69.537 1.00 24.25 1DLC4395 ATOM 4272 CD2 PHE 589 39.991 57.207 67.408 1.00 22.86 1DLC4396 ATOM 4273 CE1 PHE 589 40.658 55.638 69.592 1.00 23.24 1DLC4397 ATOM 4274 CE2 PHE 589 41.229 56.566 67.460 1.00 22.86 1DLC4398 ATOM 4275 CZ PHE 589 41.559 55.784 68.551 1.00 19.36 1DLC4399 ATOM 4276 N ASP 590 36.629 60.800 67.749 1.00 20.80 1DLC4400 ATOM 4277 CA ASP 590 35.522 61.668 67.374 1.00 21.27 1DLC4401 ATOM 4278 C ASP 590 34.286 61.011 66.776 1.00 23.02 1DLC4402 ATOM 4279 O ASP 590 34.339 59.922 66.206 1.00 24.31 1DLC4403 ATOM 4280 CB ASP 590 36.006 62.740 66.395 1.00 20.90 1DLC4404 ATOM 4281 CG ASP 590 37.235 63.476 66.887 1.00 21.49 1DLC4405 ATOM 4282 OD1 ASP 590 37.310 63.822 68.089 1.00 24.77 1DLC4406 ATOM 4283 OD2 ASP 590 38.135 63.704 66.058 1.00 25.71 1DLC4407 ATOM 4284 N LYS 591 33.170 61.722 66.905 1.00 25.19 1DLC4408 ATOM 4285 CA LYS 591 31.881 61.318 66.352 1.00 23.03 1DLC4409 ATOM 4286 C LYS 591 31.970 61.618 64.846 1.00 22.08 1DLC4410 ATOM 4287 O LYS 591 32.554 62.629 64.445 1.00 22.29 1DLC4411 ATOM 4288 CB LYS 591 30.784 62.162 67.007 1.00 25.59 1DLC4412 ATOM 4289 CG LYS 591 29.517 62.378 66.194 1.00 27.04 1DLC4413 ATOM 4290 CD LYS 591 28.657 63.423 66.891 1.00 32.39 1DLC4414 ATOM 4291 CE LYS 591 27.559 63.969 65.997 1.00 33.92 1DLC4415 ATOM 4292 NZ LYS 591 26.505 62.953 65.788 1.00 40.85 1DLC4416 ATOM 4293 N THR 592 31.460 60.726 64.008 1.00 20.83 1DLC4417 ATOM 4294 CA THR 592 31.532 60.961 62.567 1.00 21.77 1DLC4418 ATOM 4295 C THR 592 30.182 61.124 61.878 1.00 24.80 1DLC4419 ATOM 4296 O THR 592 30.114 61.669 60.778 1.00 27.91 1DLC4420 ATOM 4297 CB THR 592 32.326 59.855 61.832 1.00 20.67 1DLC4421 ATOM 4298 OG1 THR 592 31.636 58.602 61.933 1.00 18.07 1DLC4422 ATOM 4299 CG2 THR 592 33.715 59.716 62.428 1.00 20.53 1DLC4423 ATOM 4300 N ILE 593 29.113 60.643 62.510 1.00 23.91 1DLC4424 ATOM 4301 CA ILE 593 27.780 60.741 61.922 1.00 23.00 1DLC4425 ATOM 4302 C ILE 593 26.700 61.002 62.956 1.00 25.03 1DLC4426 ATOM 4303 O ILE 593 26.926 60.868 64.156 1.00 24.13 1DLC4427 ATOM 4304 CB ILE 593 27.362 59.431 61.185 1.00 20.64 1DLC4428 ATOM 4305 CG1 ILE 593 27.403 58.244 62.148 1.00 18.67 1DLC4429 ATOM 4306 CG2 ILE 593 28.219 59.189 59.962 1.00 20.92 1DLC4430 ATOM 4307 CD1 ILE 593 26.812 56.980 61.577 1.00 17.37 1DLC4431 ATOM 4308 N ASN 594 25.512 61.331 62.456 1.00 27.20 1DLC4432 ATOM 4309 CA ASN 594 24.329 61.563 63.281 1.00 30.00 1DLC4433 ATOM 4310 C ASN 594 23.472 60.305 63.268 1.00 31.97 1DLC4434 ATOM 4311 O ASN 594 23.499 59.542 62.296 1.00 32.25 1DLC4435 ATOM 4312 CB ASN 594 23.495 62.698 62.712 1.00 33.50 1DLC4436 ATOM 4313 CG ASN 594 24.047 64.042 63.059 1.00 36.33 1DLC4437 ATOM 4314 OD1 ASN 594 24.231 64.358 64.230 1.00 40.10 1DLC4438 ATOM 4315 ND2 ASN 594 24.307 64.854 62.049 1.00 37.57 1DLC4439 ATOM 4316 N LYS 595 22.708 60.084 64.335 1.00 33.91 1DLC4440 ATOM 4317 CA LYS 595 21.833 58.913 64.390 1.00 35.24 1DLC4441 ATOM 4318 C LYS 595 20.936 58.918 63.159 1.00 33.13 1DLC4442 ATOM 4319 O LYS 595 20.454 59.970 62.740 1.00 31.59 1DLC4443 ATOM 4320 CB LYS 595 20.958 58.924 65.649 1.00 38.0O 1DLC4444 ATOM 4321 CG LYS 595 21.602 58.302 66.882 1.00 45.73 1DLC4445 ATOM 4322 CD LYS 595 20.570 58.089 67.993 1.00 49.95 1DLC4446 ATOM 4323 CE LYS 595 20.323 59.344 68.835 1.00 53.81 1DLC4447 ATOM 4324 NZ LYS 595 21.391 59.568 69.861 1.00 54.01 1DLC4448 ATOM 4325 N GLY 596 20.803 57.763 62.525 1.00 34.32 1DLC4449 ATOM 4326 CA GLY 596 19.954 57.671 61.352 1.00 35.84 1DLC4450 ATOM 4327 C GLY 596 20.585 58.014 60.016 1.00 37.27 1DLC4451 ATOM 4328 O GLY 596 19.939 57.872 58.976 1.00 39.75 1DLC4452 ATOM 4329 N ASP 597 21.829 58.482 60.023 1.00 36.86 1DLC4453 ATOM 4330 CA ASP 597 22.502 58.810 58.772 1.00 33.14 1DLC4454 ATOM 4331 C ASP 597 22.864 57.551 58.002 1.00 30.98 1DLC4455 ATOM 4332 O ASP 597 23.057 56.487 58.589 1.00 30.44 1DLC4456 ATOM 4333 CB ASP 597 23.786 59.599 59.030 1.00 36.15 1DLC4457 ATOM 4334 CG ASP 597 23.530 61.040 59.404 1.00 38.83 1DLC4458 ATOM 4335 OD1 ASP 597 22.359 61.481 59.389 1.00 43.82 1DLC4459 ATOM 4336 OD2 ASP 597 24.516 61.739 59.707 1.00 41.04 1DLC4460 ATOM 4337 N THR 598 22.884 57.658 56.681 1.00 29.63 1DLC4461 ATOM 4338 CA THR 598 23.283 56.536 55.844 1.00 32.00 1DLC4462 ATOM 4339 C THR 598 24.793 56.650 55.683 1.00 28.95 1DLC4463 ATOM 4340 O THR 598 25.341 57.754 55.645 1.00 28.17 1DLC4464 ATOM 4341 CB THR 598 22.640 56.585 54.451 1.00 37.94 1DLC4465 ATOM 4342 OG1 THR 598 22.909 57.857 53.839 1.00 44.78 1DLC4466 ATOM 4343 CG2 THR 598 21.142 56.365 54.560 1.00 40.92 1DLC4467 ATOM 4344 N LEU 599 25.458 55.510 55.577 1.00 26.90 1DLC4468 ATOM 4345 CA LEU 599 26.908 55.483 55.446 1.00 24.58 1DLC4469 ATOM 4346 C LEU 599 27.476 55.735 54.049 1.00 22.87 1DLC4470 ATOM 4347 O LEU 599 27.328 54.911 53.153 1.00 24.74 1DLC4471 ATOM 4348 CB LEU 599 27.449 54.166 56.003 1.00 22.68 1DLC4472 ATOM 4349 CG LEU 599 27.957 54.118 57.449 1.00 23.90 1DLC4473 ATOM 4350 CD1 LEU 599 27.238 55.102 58.344 1.00 22.47 1DLC4474 ATOM 4351 CD2 LEU 599 27.829 52.693 57.973 1.00 23.37 1DLC4475 ATOM 4352 N THR 600 28.041 56.922 53.853 1.00 22.39 1DLC4476 ATOM 4353 CA THR 600 28.696 57.281 52.593 1.00 19.21 1DLC4477 ATOM 4354 C THR 600 30.187 57.440 52.899 1.00 19.66 1DLC4478 ATOM 4355 O THR 600 30.599 57.338 54.058 1.00 19.55 1DLC4479 ATOM 4356 CB THR 600 28.160 58.594 51.976 1.00 19.07 1DLC4480 ATOM 4357 OG1 THR 600 28.297 59.671 52.911 1.00 19.57 1DLC4481 ATOM 4358 CG2 THR 600 26.715 58.444 51.577 1.00 18.04 1DLC4482 ATOM 4359 N TYR 601 30.986 57.750 51.885 1.00 17.78 1DLC4483 ATOM 4360 CA TYR 601 32.426 57.884 52.072 1.00 17.44 1DLC4484 ATOM 4361 C TYR 601 32.891 58.710 53.278 1.00 18.41 1DLC4485 ATOM 4362 O TYR 601 33.715 58.256 54.064 1.00 18.54 1DLC4486 ATOM 4363 CB TYR 601 33.083 58.406 50.797 1.00 19.02 1DLC4487 ATOM 4364 CG TYR 601 34.576 58.213 50.799 1.00 20.72 1DLC4488 ATOM 4365 CD1 TYR 601 35.132 56.947 50.612 1.00 23.42 1DLC4489 ATOM 4366 CD2 TYR 601 35.435 59.281 51.036 1.00 20.19 1DLC4490 ATOM 4367 CE1 TYR 601 36.509 56.747 50.665 1.00 23.81 1DLC4491 ATOM 4368 CE2 TYR 601 36.809 59.098 51.094 1.00 18.57 1DLC4492 ATOM 4369 CZ TYR 601 37.344 57.830 50.910 1.00 25.85 1DLC4493 ATOM 4370 OH TYR 601 38.712 57.644 50.988 1.00 30.21 1DLC4494 ATOM 4371 N ASN 602 32.336 59.905 53.440 1.00 21.65 1DLC4495 ATOM 4372 CA ASN 602 32.721 60.789 54.539 1.00 19.54 1DLC4496 ATOM 4373 C ASN 602 32.256 60.363 55.923 1.00 18.68 1DLC4497 ATOM 4374 O ASN 602 32.600 61.003 56.913 1.00 21.51 1DLC4498 ATOM 4375 CB ASN 602 32.248 62.219 54.262 1.00 22.37 1DLC4499 ATOM 4376 CG ASN 602 33.025 62.883 53.142 1.00 28.81 1DLC4500 ATOM 4377 OD1 ASN 602 34.179 62.546 52.882 1.00 30.93 1DLC4501 ATOM 4378 ND2 ASN 602 32.393 63.830 52.466 1.00 33.11 1DLC4502 ATOM 4379 N SER 603 31.458 59.305 55.995 1.00 18.60 1DLC4503 ATOM 4380 CA SER 603 30.956 58.828 57.286 1.00 18.99 1DLC4504 ATOM 4381 C SER 603 32.080 58.199 58.101 1.00 20.18 1DLC4505 ATOM 4382 O SER 603 32.060 58.219 59.334 1.00 20.27 1DLC4506 ATOM 4383 CB SER 603 29.859 57.775 57.094 1.00 21.15 1DLC4507 ATOM 4384 OG SER 603 28.932 58.158 56.099 1.00 22.65 1DLC4508 ATOM 4385 N PHE 604 33.043 57.611 57.400 1.00 18.74 1DLC4509 ATOM 4386 CA PHE 604 34.163 56.959 58.057 1.00 21.05 1DLC4510 ATOM 4387 C PHE 604 35.337 57.874 58.345 1.00 22.35 1DLC4511 ATOM 4388 O PHE 604 35.639 58.786 57.571 1.00 25.60 1DLC4512 ATOM 4389 CB PHE 604 34.642 55.761 57.243 1.00 17.33 1DLC4513 ATOM 4390 CG PHE 604 33.728 54.589 57.318 1.00 19.46 1DLC4514 ATOM 4391 CD1 PHE 604 32.615 54.504 56.478 1.00 20.57 1DLC4515 ATOM 4392 CD2 PHE 604 33.955 53.584 58.251 1.00 18.69 1DLC4516 ATOM 4393 CE1 PHE 604 31.735 53.435 56.568 1.00 21.99 1DLC4517 ATOM 4394 CE2 PHE 604 33.090 52.505 58.359 1.00 21.18 1DLC4518 ATOM 4395 CZ PHE 604 31.971 52.426 57.515 1.00 25.90 1DLC4519 ATOM 4396 N ASN 605 35.994 57.610 59.470 1.00 21.14 1DLC4520 ATOM 4397 CA ASN 605 37.168 58.359 59.890 1.00 19.17 1DLC4521 ATOM 4398 C ASN 605 38.294 57.351 60.132 1.00 17.19 1DLC4522 ATOM 4399 O ASN 605 38.033 56.195 60.457 1.00 13.48 1DLC4523 ATOM 4400 CB ASN 605 36.866 59.139 61.172 1.00 20.09 1DLC4524 ATOM 4401 CG ASN 605 38.083 59.882 61.715 1.00 24.94 1DLC4525 ATOM 4402 OD1 ASN 605 38.877 60.446 60.961 1.00 23.59 1DLC4526 ATOM 4403 ND2 ASN 605 38.230 59.886 63.029 1.00 23.22 1DLC4527 ATOM 4404 N LEU 606 39.529 57.768 59.862 1.00 15.78 1DLC4528 ATOM 4405 CA LEU 606 40.706 56.929 60.085 1.00 15.38 1DLC4529 ATOM 4406 C LEU 606 41.546 57.666 61.109 1.00 14.32 1DLC4530 ATOM 4407 O LEU 606 42.089 58.723 60.824 1.00 19.53 1DLC4531 ATOM 4408 CB LEU 606 41.512 56.726 58.803 1.00 11.43 1DLC4532 ATOM 4409 CG LEU 606 42.691 55.748 58.912 1.00 13.17 1DLC4533 ATOM 4410 CD1 LEU 606 42.188 54.310 59.013 1.00 8.03 1DLC4534 ATOM 4411 CD2 LEU 606 43.591 55.891 57.712 1.00 11.28 1DLC4535 ATOM 4412 N ALA 607 41.610 57.132 62.316 1.00 14.53 1DLC4536 ATOM 4413 CA ALA 607 42.357 57.785 63.376 1.00 17.06 1DLC4537 ATOM 4414 C ALA 607 43.361 56.866 64.075 1.00 18.57 1DLC4538 ATOM 4415 O ALA 607 43.101 55.678 64.277 1.00 21.74 1DLC4539 ATOM 4416 CB ALA 607 41.391 58.389 64.386 1.00 14.48 1DLC4540 ATOM 4417 N SER 608 44.512 57.429 64.425 1.00 18.31 1DLC4541 ATOM 4418 CA SER 608 45.581 56.695 65.105 1.00 19.59 1DLC4542 ATOM 4419 C SER 608 45.444 56.664 66.617 1.00 19.21 1DLC4543 ATOM 4420 O SER 608 44.771 57.504 67.214 1.00 22.53 1DLC4544 ATOM 4421 CB SER 608 46.940 57.343 64.817 1.00 17.65 1DLC4545 ATOM 4422 OG SER 608 47.288 57.266 63.450 1.00 31.60 1DLC4546 ATOM 4423 N PHE 609 46.064 55.669 67.231 1.00 19.10 1DLC4547 ATOM 4424 CA PHE 609 46.111 55.593 68.687 1.00 20.56 1DLC4548 ATOM 4425 C PHE 609 47.461 56.260 68.959 1.00 23.47 1DLC4549 ATOM 4426 O PHE 609 48.405 56.100 68.173 1.00 24.46 1DLC4550 ATOM 4427 CB PHE 609 46.158 54.144 69.179 1.00 18.14 1DLC4551 ATOM 4428 CG PHE 609 44.822 53.470 69.239 1.00 13.91 1DLC4552 ATOM 4429 CD1 PHE 609 44.213 52.994 68.082 1.00 14.21 1DLC4553 ATOM 4430 CD2 PHE 609 44.183 53.288 70.461 1.00 12.55 1DLC4554 ATOM 4431 CE1 PHE 609 42.990 52.348 68.144 1.00 13.77 1DLC4555 ATOM 4432 CE2 PHE 609 42.962 52.643 70.538 1.00 13.77 1DLC4556 ATOM 4433 CZ PHE 609 42.361 52.170 69.378 1.00 16.49 1DLC4557 ATOM 4434 N SER 610 47.568 56.983 70.063 1.00 26.13 1DLC4558 ATOM 4435 CA SER 610 48.810 57.686 70.408 1.00 30.80 1DLC4559 ATOM 4436 C SER 610 50.092 56.849 70.539 1.00 29.67 1DLC4560 ATOM 4437 O SER 610 51.025 56.975 69.748 1.00 30.28 1DLC4561 ATOM 4438 CB SER 610 48.604 58.473 71.708 1.00 34.50 1DLC4562 ATOM 4439 OG SER 610 48.026 57.642 72.714 1.00 42.82 1DLC4563 ATOM 4440 N THR 611 50.101 55.983 71.542 1.00 30.68 1DLC4564 ATOM 4441 CA THR 611 51.235 55.137 71.900 1.00 33.04 1DLC4565 ATOM 4442 C THR 611 51.547 53.913 71.043 1.00 32.68 1DLC4566 ATOM 4443 O THR 611 50.639 53.244 70.553 1.00 35.44 1DLC4567 ATOM 4444 CB THR 611 51.037 54.639 73.347 1.00 35.70 1DLC4568 ATOM 4445 OG1 THR 611 50.549 55.722 74.151 1.00 37.55 1DLC4569 ATOM 4446 CG2 THR 611 52.351 54.133 73.943 1.00 41.55 1DLC4570 ATOM 4447 N PRO 612 52.850 53.613 70.849 1.00 30.50 1DLC4571 ATOM 4449 C PRO 612 53.382 51.236 70.982 1.00 25.09 1DLC4573 ATOM 4450 O PRO 612 53.513 51.361 72.203 1.00 24.09 1DLC4574 ATOM 4451 CB PRO 612 54.795 52.883 69.733 1.00 24.58 1DLC4575 ATOM 4452 CG PRO 612 54.792 54.370 69.890 1.00 30.13 1DLC4576 ATOM 4453 CD PRO 612 53.935 54.574 71.102 1.00 29.34 1DLC4577 ATOM 4454 N PHE 613 53.334 50.048 70.389 1.00 22.86 1DLC4578 ATOM 4455 CA PHE 613 53.317 48.813 71.170 1.00 16.75 1DLC4579 ATOM 4456 C PHE 613 53.921 47.629 70.413 1.00 19.20 1DLC4580 ATOM 4457 O PHE 613 54.063 47.673 69.198 1.00 19.97 1DLC4581 ATOM 4458 CB PHE 613 51.861 48.483 71.518 1.00 17.73 1DLC4582 ATOM 4459 CG PHE 613 50.976 48.303 70.305 1.00 17.53 1DLC4583 ATOM 4460 CD1 PHE 613 50.844 47.050 69.699 1.00 15.34 1DLC4584 ATOM 4461 CD2 PHE 613 50.316 49.392 69.741 1.00 15.52 1DLC4585 ATOM 4462 CE1 PHE 613 50.075 46.884 68.550 1.00 18.54 1DLC4586 ATOM 4463 CE2 PHE 613 49.542 49.242 68.591 1.00 18.60 1DLC4587 ATOM 4464 CZ PHE 613 49.420 47.985 67.991 1.00 19.20 1DLC4588 ATOM 4465 N GLU 614 54.252 46.565 71.136 1.00 22.92 1DLC4589 ATOM 4466 CA GLU 614 54.788 45.344 70.521 1.00 28.15 1DLC4590 ATOM 4467 C GLU 614 53.683 44.278 70.508 1.00 26.61 1DLC4591 ATOM 4468 G GLU 614 52.791 44.305 71.357 1.00 28.65 1DLC4592 ATOM 4469 CB GLU 614 55.922 44.758 71.352 1.00 34.57 1DLC4593 ATOM 4470 CG GLU 614 57.135 45.603 71.583 1.00 41.25 1DLC4594 ATOM 4471 CD GLU 614 58.068 44.932 72.583 1.00 48.16 1DLC4595 ATOM 4472 OE1 GLU 614 58.144 43.675 72.601 1.00 49.77 1DLC4596 ATOM 4473 OE2 GLU 614 58.706 45.662 73.370 1.00 53.23 1DLC4597 ATOM 4474 N LEU 615 53.773 43.303 69.608 1.00 26.20 1DLC4598 ATOM 4475 CA LEU 615 52.774 42.238 69.558 1.00 25.30 1DLC4599 ATOM 4476 C LEU 615 53.175 41.073 70.455 1.00 27.80 1DLC4600 ATOM 4477 O LEU 615 53.465 39.975 69.982 1.00 30.45 1DLC4601 ATOM 4478 CB LEU 615 52.558 41.746 68.128 1.00 24.01 1DLC4602 ATOM 4479 CG LEU 615 51.781 42.673 67.196 1.00 27.00 1DLC4603 ATOM 4480 CD1 LEU 615 51.591 41.995 65.850 1.00 26.98 1DLC4604 ATOM 4481 CD2 LEU 615 50.431 43.015 67.805 1.00 26.72 1DLC4605 ATOM 4482 N SER 616 53.162 41.311 71.759 1.00 28.53 1DLC4606 ATOM 4483 CA SER 616 53.525 40.292 72.744 1.00 34.72 1DLC4607 ATOM 4484 C SER 616 52.371 39.325 73.044 1.00 37.29 1DLC4608 ATOM 4485 O SER 616 52.207 38.865 74.183 1.00 40.69 1DLC4609 ATOM 4486 CB SER 616 53.957 40.975 74.042 1.00 38.38 1DLC4610 ATOM 4487 OG SER 616 52.908 41.795 74.545 1.00 40.32 1DLC4611 ATOM 4488 N GLY 617 51.575 39.027 72.021 1.00 35.36 1DLC4612 ATOM 4489 CA GLY 617 50.439 38.139 72.175 1.00 28.58 1DLC4613 ATOM 4490 C GLY 617 49.746 37.935 70.846 1.00 27.52 1DLC4614 ATOM 4491 O GLY 617 50.171 38.483 69.832 1.00 27.48 1DLC4615 ATOM 4492 N ASN 618 48.673 37.152 70.836 1.00 26.58 1DLC4616 ATOM 4493 CA ASN 618 47.958 36.898 69.588 1.00 25.03 1DLC4617 ATOM 4494 C ASN 618 46.514 37.351 69.564 1.00 22.65 1DLC4618 ATOM 4495 O ASN 618 45.993 37.679 68.513 1.00 24.08 1DLC4619 ATOM 4496 CB ASN 618 47.991 35.414 69.237 1.00 25.99 1DLC4620 ATOM 4497 CG ASN 618 49.388 34.872 69.126 1.00 27.81 1DLC4621 ATOM 4498 OD1 ASN 618 49.858 34.163 70.014 1.00 32.06 1DLC4622 ATOM 4499 ND2 ASN 618 50.060 35.191 68.038 1.00 28.41 1DLC4623 ATOM 4500 N ASN 619 45.857 37.337 70.711 1.00 21.28 1DLC4624 ATOM 4501 CA ASN 619 44.453 37.718 70.766 1.00 23.58 1DLC4625 ATOM 4502 C ASN 619 44.187 39.189 70.986 1.00 23.07 1DLC4626 ATOM 4503 O ASN 619 44.182 39.670 72.118 1.00 23.17 1DLC4627 ATOM 4504 CB ASN 619 43.718 36.886 71.808 1.00 24.66 1DLC4628 ATOM 4505 CG ASN 619 43.780 35.423 71.500 1.00 26.16 1DLC4629 ATOM 4506 OD1 ASN 619 42.964 34.912 70.754 1.00 30.61 1DLC4630 ATOM 4507 ND2 ASN 619 44.790 34.747 72.020 1.00 27.81 1DLC4631 ATOM 4508 N LEU 620 43.962 39.897 69.888 1.00 24.96 1DLC4632 ATOM 4509 CA LEU 620 43.681 41.320 69.938 1.00 24.70 1DLC4633 ATOM 4510 C LEU 620 42.184 41.557 70.168 1.00 26.87 1DLC4634 ATOM 4511 O LEU 620 41.332 41.071 69.421 1.00 26.49 1DLC4635 ATOM 4512 CB LEU 620 44.132 41.996 68.640 1.00 21.52 1DLC4636 ATOM 4513 CG LEU 620 43.980 43.521 68.582 1.00 21.06 1DLC4637 ATOM 4514 CD1 LEU 620 44.827 44.159 69.665 1.00 22.05 1DLC4638 ATOM 4515 CD2 LEU 620 44.383 44.042 67.220 1.00 19.94 1DLC4639 ATOM 4516 N GLN 621 41.871 42.295 71.222 1.00 26.81 1DLC4640 ATOM 4517 CA GLN 621 40.490 42.606 71.533 1.00 28.41 1DLC4641 ATOM 4518 C GLN 621 40.238 44.107 71.450 1.0G 27.09 1DLC4642 ATOM 4519 O GLN 621 41.003 44.909 71.987 1.00 26.35 1DLC4643 ATOM 4520 CB GLN 621 40.127 42.097 72.926 1.00 30.85 1DLC4644 ATOM 4521 CG GLN 621 38.687 42.369 73.303 1.00 38.10 1DLC4645 ATOM 4522 CD GLN 621 38.395 42.019 74.741 1.00 42.94 1DLC4646 ATOM 4523 OE1 GLN 621 38.025 40.885 75.054 1.00 46.82 1DLC4647 ATOM 4524 NE2 GLN 621 38.573 42.984 75.635 1.00 43.76 1DLC4648 ATOM 4525 N ILE 622 39.193 44.480 70.723 1.00 27.04 1DLC4649 ATOM 4526 CA ILE 622 38.819 45.881 70.585 1.00 24.51 1DLC4650 ATOM 4527 C ILE 622 37.571 46.089 71.440 1.00 23.99 1DLC4651 ATOM 4528 O ILE 622 36.602 45.342 71.329 1.00 24.51 1DLC4652 ATOM 4529 CB ILE 622 38.491 46.269 69.113 1.00 25.00 1DLC4653 ATOM 4530 CG1 ILE 622 39.637 45.890 68.169 1.00 25.97 1DLC4654 ATOM 4531 CG2 ILE 622 38.266 47.772 69.005 1.00 22.97 1DLC4655 ATOM 4532 CD1 ILE 622 39.668 44.433 67.761 1.00 32.60 1DLC4656 ATOM 4533 N GLY 623 37.615 47.075 72.323 1.00 24.24 1DLC4657 ATOM 4534 CA GLY 623 36.476 47.360 73.178 1.00 23.29 1DLC4658 ATOM 4535 C GLY 623 36.019 48.798 72.985 1.00 27.25 1DLC4659 ATOM 4536 O GLY 623 36.825 49.682 72.673 1.00 28.11 1DLC4660 ATOM 4537 N VAL 624 34.731 49.048 73.184 1.00 26.21 1DLC4661 ATOM 4538 CA VAL 624 34.19T 50.390 73.009 1.00 24.65 1DLC4662 ATOM 4539 C VAL 624 33.390 50.847 74.217 1.00 25.91 1DLC4663 ATOM 4540 O VAL 624 32.695 50.060 74.854 1.00 28.03 1DLC4664 ATOM 4541 CB VAL 624 33.252 50.470 71.780 1.00 22.56 1DLC4665 ATOM 4542 CG1 VAL 624 33.075 51.903 71.367 1.00 21.19 1DLC4666 ATOM 4543 CG2 VAL 624 33.774 49.633 70.624 1.00 24.76 1DLC4667 ATOM 4544 N THR 625 33.528 52.117 74.564 1.00 25.09 1DLC4668 ATOM 4545 CA THR 625 32.755 52.693 75.653 1.00 24.39 1DLC4669 ATOM 4546 C THR 625 32.428 54.119 75.281 1.00 24.42 1DLC4670 ATOM 4547 O THR 625 33.051 54.700 74.387 1.00 22.03 1DLC4671 ATOM 4548 CB THR 625 33.473 52.690 77.007 1.00 24.18 1DLC4672 ATOM 4549 OG1 THR 625 34.753 53.312 76.877 1.00 30.48 1DLC4673 ATOM 4550 CG2 THR 625 33.610 51.271 77.544 1.00 25.23 1DLC4674 ATOM 4551 N GLY 626 31.432 54.672 75.956 1.00 28.18 1DLC4675 ATOM 4552 CA GLY 626 31.015 56.034 75.672 1.00 29.72 1DLC4676 ATOM 4553 C GLY 626 29.721 56.089 74.881 1.00 30.01 1DLC4677 ATOM 4554 O GLY 626 29.311 57.162 74.438 1.00 34.83 1DLC4678 ATOM 4555 N LEU 627 29.102 54.931 74.668 1.00 27.34 1DLC4679 ATOM 4556 CA LEU 627 27.840 54.852 73.946 1.00 28.54 1DLC4680 ATOM 4557 C LEU 627 26.655 55.102 74.872 1.00 31.09 1DLC4681 ATOM 4558 O LEU 627 26.687 54.772 76.058 1.00 32.97 1DLC4682 ATOM 4559 CB LEU 627 27.668 53.483 73.288 1.00 25.31 1DLC4683 ATOM 4560 CG LEU 627 28.673 53.087 72.211 1.00 24.90 1DLC4684 ATOM 4561 CD1 LEU 627 28.212 51.813 71.544 1.00 25.05 1DLC4685 ATOM 4562 CD2 LEU 627 28.784 54.196 71.185 1.00 26.40 1DLC4686 ATOM 4563 N SER 628 25.619 55.711 74.316 1.00 33.11 1DLC4687 ATOM 4564 CA SER 628 24.390 56.000 75.038 1.00 32.54 1DLC4688 ATOM 4565 C SER 628 23.306 55.280 74.259 1.00 34.13 1DLC4689 ATOM 4566 O SER 628 23.539 54.854 73.126 1.00 34.40 1DLC4690 ATOM 4567 CB SER 628 24.108 57.500 75.031 1.00 34.45 1DLC4691 ATOM 4568 OG SER 628 25.205 58.224 75.563 1.00 43.41 1DLC4692 ATOM 4569 N ALA 629 22.121 55.141 74.842 1.00 36.19 1DLC4693 ATOM 4570 CA ALA 629 21.026 54.462 74.149 1.00 35.18 1DLC4694 ATOM 4571 C ALA 629 20.802 55.085 72.769 1.00 32.86 1DLC4695 ATOM 4572 O ALA 629 20.722 56.307 72.632 1.00 33.61 1DLC4696 ATOM 4573 CB ALA 629 19.753 54.536 74.977 1.00 38.53 1DLC4697 ATOM 4574 N GLY 630 20.776 54.250 71.739 1.00 31.19 1DLC4698 ATOM 4575 CA GLY 630 20.572 54.767 70.397 1.00 31.13 1DLC4699 ATOM 4576 C GLY 630 21.845 55.068 69.625 1.00 30.12 1DLC4700 ATOM 4577 O GLY 630 21.797 55.416 68.440 1.00 29.53 1DLC4701 ATOM 4578 N ASP 631 22.984 54.975 70.303 1.00 29.51 1DLC4702 ATOM 4579 CA ASP 631 24.269 55.204 69.658 1.00 29.05 1DLC4703 ATOM 4580 C ASP 631 24.772 53.950 68.958 1.00 26.70 1DLC4704 ATOM 4581 O ASP 631 24.535 52.834 69.409 1.00 25.70 1DLC4705 ATOM 4582 CB ASP 631 25.315 55.686 70.662 1.00 30.55 1DLC4706 ATOM 4583 CG ASP 631 25.248 57.175 70.902 1.00 29.06 1DLC4707 ATOM 4584 OD1 ASP 631 24.974 57.917 69.940 1.00 32.20 1DLC4708 ATOM 4585 OD2 ASP 631 25.480 57.608 72.050 1.00 32.19 1DLC4709 ATOM 4586 N LYS 632 25.448 54.155 67.836 1.00 27.29 1DLC4710 ATOM 4587 CA LYS 632 26.001 53.063 67.043 1.00 28.14 1DLC4711 ATOM 4588 C LYS 632 27.423 53.376 66.582 1.00 28.21 1DLC4712 ATOM 4589 O LYS 632 27.751 54.529 66.259 1.00 27.32 1DLC4713 ATOM 4590 CB LYS 632 25.144 52.822 65.796 1.00 30.56 1DLC4714 ATOM 4591 CG LYS 632 24.302 51.570 65.808 1.00 34.27 1DLC4715 ATOM 4592 CD LYS 632 22.833 51.929 65.849 1.00 38.40 1DLC4716 ATOM 4593 CE LYS 632 21.989 50.859 65.198 1.00 38.52 1DLC4717 ATOM 4594 NZ LYS 632 22.334 50.732 63.756 1.00 39.82 1DLC4718 ATOM 4595 N VAL 633 28.257 52.337 66.557 1.00 27.38 1DLC4719 ATOM 4596 CA VAL 633 29.644 52.437 66.097 1.00 21.96 1DLC4720 ATOM 4597 C VAL 633 29.876 51.322 65.082 1.00 20.64 1DLC4721 ATOM 4598 O VAL 633 29.526 50.173 65.324 1.00 16.03 1DLC4722 ATOM 4599 CB VAL 633 30.665 52.281 67.244 1.00 20.74 1DLC4723 ATOM 4600 CG1 VAL 633 32.082 52.371 66.701 1.00 21.42 1DLC4724 ATOM 4601 CG2 VAL 633 30.462 53.360 68.275 1.00 21.81 1DLC4725 ATOM 4602 N TYR 634 30.393 51.687 63.917 1.00 21.62 1DLC4726 ATOM 4603 CA TYR 634 30.687 50.729 62.859 1.00 19.61 1DLC4727 ATOM 4604 C TYR 634 32.199 50.649 62.704 1.00 20.81 1DLC4728 ATOM 4605 O TYR 634 32.872 51.675 62.583 1.00 19.65 1DLC4729 ATOM 4606 CB TYR 634 30.072 51.188 61.541 1.00 20.60 1DLC4730 ATOM 4607 CG TYR 634 28.582 51.418 61.612 1.00 24.53 1DLC4731 ATOM 4608 CD1 TYR 634 28.069 52.660 61.978 1.00 22.76 1DLC4732 ATOM 4609 CD2 TYR 634 27.684 50.392 61.306 1.00 24.10 1DLC4733 ATOM 4610 CE1 TYR 634 26.713 52.877 62.036 1.00 26.60 1DLC4734 ATOM 4611 CE2 TYR 634 26.321 50.598 61.359 1.00 24.93 1DLC4735 ATOM 4612 CZ TYR 634 25.839 51.845 61.723 1.00 29.72 1DLC4736 ATOM 4613 OH TYR 634 24.481 52.074 61.754 1.00 34.36 1DLC4737 ATOM 4614 N ILE 635 32.741 49.438 62.750 1.00 20.73 1DLC4738 ATOM 4615 CA ILE 635 34.182 49.257 62.602 1.00 18.75 1DLC4739 ATOM 4616 C ILE 635 34.474 48.479 61.340 1.00 16.63 1DLC4740 ATOM 4617 O ILE 635 33.941 47.398 61.115 1.00 17.24 1DLC4741 ATOM 4618 CB ILE 635 34.811 48.520 63.794 1.00 20.45 1DLC4742 ATOM 4619 CG1 ILE 635 34.344 49.147 65.119 1.00 22.26 1DLC4743 ATOM 4620 CG2 ILE 635 36.329 48.591 63.692 1.00 22.68 1DLC4744 ATOM 4621 CD1 ILE 635 34.684 48.321 66.359 1.00 21.31 1DLC4745 ATOM 4622 N ASP 636 35.302 49.070 60.499 1.00 17.78 1DLC4746 ATOM 4623 CA ASP 636 35.683 48.464 59.241 1.00 17.49 1DLC4747 ATOM 4624 C ASP 636 36.993 47.673 59.370 1.00 18.04 1DLC4748 ATOM 4625 O ASP 636 37.003 46.440 59.251 1.00 17.98 1DLC4749 ATOM 4626 CB ASP 636 35.802 49.561 58.170 1.00 15.99 1DLC4750 ATOM 4627 CG ASP 636 36.303 49.036 56.842 1.00 18.79 1DLC4751 ATOM 4628 OD1 ASP 636 35.898 47.926 56.440 1.00 25.68 1DLC4752 ATOM 4629 OD2 ASP 636 37.109 48.733 56.197 1.00 18.48 1DLC4753 ATOM 4630 N LYS 637 38.083 48.381 59.670 1.00 18.05 1DLC4754 ATOM 4631 CA LYS 637 39.402 47.758 59.775 1.00 16.49 1DLC4755 ATOM 4632 C LYS 637 40.305 48.342 60.846 1.00 15.84 1DLC4756 ATOM 4633 O LYS 637 40.099 49.462 61.305 1.00 19.42 1DLC4757 ATOM 4634 CB LYS 637 40.153 47.887 58.441 1.00 13.95 1DLC4758 ATOM 4635 CG LYS 637 39.432 47.343 57.217 1.00 15.81 1DLC4759 ATOM 4636 CD LYS 637 40.290 47.503 55.987 1.00 15.16 1DLC4760 ATOM 4637 CE LYS 637 39.562 47.083 54.729 1.00 18.94 1DLC4761 ATOM 4638 NZ LYS 637 38.566 48.094 54.290 1.00 25.98 1DLC4762 ATOM 4639 N ILE 638 41.285 47.547 61.255 1.00 17.01 1DLC4763 ATOM 4640 CA ILE 638 42.312 47.967 62.205 1.00 18.44 1DLC4764 ATOM 4641 C ILE 638 43.590 47.876 61.359 1.00 18.91 1DLC4765 ATOM 4642 O ILE 638 43.728 46.979 60.528 1.00 17.29 1DLC4766 ATOM 4643 CB ILE 638 42.402 47.038 63.455 1.00 19.92 1DLC4767 ATOM 4644 CG1 ILE 638 43.633 47.371 64.303 1.00 23.39 1DLC4768 ATOM 4645 CG2 ILE 638 42.467 45.589 63.051 1.00 22.91 1DLC4769 ATOM 4646 CD1 ILE 638 43.463 48.546 65.222 1.00 25.42 1DLC4770 ATOM 4647 N GLU 639 44.452 48.876 61.467 1.00 19.60 1DLC4771 ATOM 4648 CA GLU 639 45.693 48.893 60.699 1.00 19.14 1DLC4772 ATOM 4649 C GLU 639 46.903 48.901 61.614 1.00 19.79 1DLC4773 ATOM 4650 O GLU 639 46.878 49.481 62.704 1.00 20.61 1DLC4774 ATOM 4651 CB GLU 639 45.772 50.131 59.807 1.00 21.25 1DLC4775 ATOM 4652 CG GLU 639 44.596 50.362 58.880 1.00 20.87 1DLC4776 ATOM 4653 CD GLU 639 44.831 51.536 57.938 1.00 21.31 1DLC4777 ATOM 4654 OE1 GLU 639 45.626 52.437 58.270 1.00 23.01 1DLC4778 ATOM 4655 OE2 GLU 639 44.225 51.560 56.853 1.00 23.98 1DLC4779 ATOM 4656 N PHE 640 47.969 48.259 61.162 1.00 18.90 1DLC4780 ATOM 4657 CA PHE 640 49.193 48.212 61.940 1.00 18.35 1DLC4781 ATOM 4658 C PHE 640 50.310 48.862 61.154 1.00 18.44 1DLC4782 ATOM 4659 O PHE 640 50.542 48.535 59.986 1.00 19.24 1DLC4783 ATOM 4660 CB PHE 640 49.552 46.775 62.303 1.00 18.10 1DLC4784 ATOM 4661 CG PHE 640 48.503 46.086 63.121 1.00 19.75 1DLC4785 ATOM 4662 CD1 PHE 640 47.457 45.408 62.504 1.00 22.39 1DLC4786 ATOM 4663 CD2 PHE 640 48.548 46.122 64.508 1.00 21.02 1DLC4787 ATOM 4664 CE1 PHE 640 64.471 44.774 63.260 1.00 23.22 1DLC4788 ATOM 4665 CE2 PHE 640 47.562 45.488 65.275 1.00 20.83 1DLC4789 ATOM 4666 CZ PHE 640 46.528 44.816 64.649 1.00 21.24 1DLC4790 ATOM 4667 N ILE 641 50.935 49.855 61.773 1.00 18.54 1DLC4791 ATOM 4668 CA ILE 641 52.032 50.574 61.148 1.00 17.65 1DLC4792 ATOM 4669 C ILE 641 53.354 50.254 61.825 1.00 18.10 1DLC4793 ATOM 4670 O ILE 641 53.532 50.515 63.020 1.00 16.34 1DLC4794 ATOM 4671 CB ILE 641 51.806 52.098 61.187 1.00 19.28 1DLC4795 ATOM 4672 CG1 ILE 641 50.490 52.443 60.484 1.00 16.97 1DLC4796 ATOM 4673 CG2 ILE 641 52.994 52.823 60.536 1.00 16.12 1DLC4797 ATOM 4674 CD1 ILE 641 50.125 53.890 60.562 1.00 20.58 1DLC4798 ATOM 4675 N PRO 642 54.270 49.611 61.084 1.00 21.02 1DLC4799 ATOM 4676 CA PRO 642 55.590 49.252 61.616 1.00 22.98 1DLC4800 ATOM 4677 C PRO 642 56.315 50.542 61.966 1.00 24.81 1DLC4801 ATOM 4678 O PRO 642 56.451 51.442 61.131 1.00 29.36 1DLC4802 ATOM 4679 CB PRO 642 56.237 48.499 60.453 1.00 20.26 1DLC4803 ATOM 4680 CG PRO 642 55.532 49.048 59.237 1.00 23.90 1DLC4804 ATOM 4681 CD PRO 642 54.113 49.142 59.697 1.00 21.85 1DLC4805 ATOM 4682 N VAL 643 56.741 50.647 63.216 1.00 27.45 1DLC4806 ATOM 4683 CA VAL 643 57.389 51.859 63.694 1.00 31.83 1DLC4807 ATOM 4684 C VAL 643 58.701 51.581 64.435 1.00 36.92 1DLC4808 ATOM 4685 O VAL 643 58.839 50.545 65.083 1.00 41.24 1DLC4809 ATOM 4686 CB VAL 643 56.372 52.642 64.579 1.00 29.35 1DLC4810 ATOM 4687 CG1 VAL 643 56.972 53.075 65.901 1.00 25.64 1DLC4811 ATOM 4688 CG2 VAL 643 55.810 53.807 63.806 1.00 21.99 1DLC4812 ATOM 4689 N ASN 644 59.668 52.487 64.301 1.00 41.01 1DLC4813 ATOM 4690 CA ASN 644 60.962 52.336 64.973 1.00 46.63 1DLC4814 ATOM 4691 C ASN 644 60.972 52.790 66.436 1.00 49.51 1DLC4815 ATOM 4692 O ASN 644 60.080 53.575 66.835 1.00 52.85 1DLC4816 ATOM 4693 CB ASN 644 62.067 53.061 64.204 1.00 45.33 1DLC4817 ATOM 4694 CG ASN 644 62.467 52.332 62.940 1.00 48.91 1DLC4818 ATOM 4695 OD1 ASN 644 62.868 52.952 61.955 1.00 51.43 1DLC4819 ATOM 4696 ND2 ASN 644 62.365 51.008 62.957 1.00 48.98 1DLC4820 ATOM 4697 OXT ASN 644 61.887 52.354 67.174 1.00 54.29 1DLC4821 TER 4698 ASN 644 1DLC4822 HETATM 4699 O HOH 1 28.158 56.658 35.558 1.00 15.93 1DLC4823 HETATM 4700 O HOH 2 30.007 42.529 51.310 1.00 29.97 1DLC4824 HETATM 4701 O HOH 3 36.424 37.532 49.700 1.00 18.65 1DLC4825 HETATM 4702 O HOH 4 37.001 54.392 48.062 1.00 10.97 1DLC4826 HETATM 4703 O HOH 5 41.124 51.393 35.747 1.00 18.84 1DLC4827 HETATM 4704 O HOH 6 39.377 60.985 65.970 1.00 19.48 1DLC4828 HETATM 4705 O HOH 7 26.260 28.918 41.587 1.00 14.99 1DLC4829 HETATM 4706 O HOH 8 33.639 33.867 54.596 1.00 15.88 1DLC4830 HETATM 4707 O HOH 9 51.981 45.967 59.702 1.00 20.77 1DLC4831 HETATM 4708 O HOH 10 49.865 76.628 42.176 1.00 46.98 1DLC4832 HETATM 4709 O HOH 11 56.250 42.866 68.444 1.00 32.76 1DLC4833 HETATM 4710 O HOH 12 48.128 58.353 60.425 1.00 13.12 1DLC4834 HETATM 4711 O HOH 13 39.909 31.847 39.167 1.00 22.65 1DLC4835 HETATM 4712 O HOH 14 42.525 40.309 74.464 1.00 21.75 1DLC4836 HETATM 4713 O HOH 15 35.320 44.237 58.596 1.00 20.02 1DLC4837 HETATM 4714 O HOH 16 42.939 58.321 46.818 1.00 20.43 1DLC4838 HETATM 4715 O HOH 17 34.791 45.871 55.097 1.00 17.61 1DLC4839 HETATM 4716 O HOH 18 59.791 70.818 25.850 1.00 58.06 1DLC4840 HETATM 4717 O HOH 19 49.421 53.503 45.093 1.00 28.93 1DLC4841 HETATM 4718O HOH 20 26.124 35.366 50.587 1.00 20.75 1DLC4842 HETATM 4719 O HOH 21 22.215 55.259 63.293 1.00 55.44 1DLC4843 HETATM 4720 O HOH 22 29.336 36.466 34.470 1.00 28.07 1DLC4844 HETATM 4721 O HOH 23 36.856 28.647 51.651 1.00 25.28 1DLC4845 HETATM 4722 O HOH 24 32.887 40.556 54.227 1.00 18.71 1DLC4846 HETATM 4723 O HOH 25 11.473 29.145 36.339 1.00 30.31 1DLC4847 HETATM 4724 O HOH 26 29.975 51.053 31.090 1.00 24.69 1DLC4848 HETATM 4725 O HOH 27 23.211 34.799 38.939 1.00 18.55 1DLC4849 HETATM 4726 O HOH 28 40.839 35.888 64.000 1.00 20.47 1DLC4850 HETATM 4727 O HOH 29 48.014 63.906 44.198 1.00 20.94 1DLC4851 HETATM 4728 O HOH 30 38.825 30.321 41.019 1.00 17.31 1DLC4852 HETATM 4729 O HOH 31 43.802 60.051 66.555 1.00 21.11 1DLC4853 HETATM 4730 O HOH 32 38.144 26.579 49.130 1.00 19.35 1DLC4854 HETATM 4731 O HOH 33 38.268 41.944 41.244 1.00 29.87 1DLC4855 HETATM 4732 O HOH 34 37.512 21.444 38.474 1.00 24.99 1DLC4856 HETATM 4733 O HOH 35 32.702 36.732 53.626 1.00 20.86 1DLC4857 HETATM 4734 O HOH 36 49.899 63.801 28.431 1.00 28.04 1DLC4858 HETATM 4735 O HOH 37 49.371 53.132 68.181 1.00 26.75 1DLC4859 HETATM 4736 O HOH 38 29.606 38.319 55.430 1.00 25.89 1DLC4860 HETATM 4737 O HOH 39 41.950 72.970 42.722 1.00 27.25 1DLC4861 HETATM 4738 O HOH 40 39.554 70.091 45.032 1.00 44.51 1DLC4862 HETATM 4739 O HOH 41 43.093 57.590 52.155 1.00 22.06 1DLC4863 HETATM 4740 O HOH 42 36.402 31.325 52.356 1.00 14.91 1DLC4864 HETATM 4741 O HOH 43 42.564 71.403 44.910 1.00 26.89 1DLC4865 HETATM 4742 O HOH 44 31.202 36.895 36.508 1.00 20.87 1DLC4866 HETATM 4743 O HOH 45 9.974 36.335 44.772 1.00 23.38 1DLC4867 HETATM 4744 O HOH 46 17.109 18.398 39.762 1.00 24.03 1DLC4868 HETATM 4745 O HOH 47 26.895 37.648 43.823 1.00 21.28 1DLC4869 HETATM 4746 O HOH 48 19.711 22.004 38.604 1.00 24.53 1DLC4870 HETATM 4747 O HOH 49 37.262 44.313 53.204 1.00 43.74 1DLC4871 HETATM 4748 O HOH 50 33.936 47.399 47.859 1.00 22.31 1DLC4872 HETATM 4749 O HOH 51 30.403 46.461 72.142 1.00 32.70 1DLC4873 HETATM 4750 O HOH 52 46.001 19.419 46.812 1.00 40.72 1DLC4874 HETATM 4751 O HOH 53 45.816 40.175 53.356 1.00 25.45 1DLC4875 HETATM 4752O HOH 54 30.264 60.779 51.534 1.00 25.95 1DLC4876 HETATM 4753 O HOH 55 10.154 28.983 45.206 1.00 22.19 1DLC4877 HETATM 4754 O HOH 56 28.704 26.404 57.946 1.00 26.44 1DLC4878 HETATM 4755 O HOH 57 32.699 38.030 55.930 1.00 23.26 1DLC4879 HETATM 4756 O HOH 58 14.955 11.719 28.113 1.00 48.40 1DLC4880 HETATM 4757 O HOH 59 18.793 41.375 48.389 1.00 46.53 1DLC4881 HETATM 4758 O HOH 60 36.654 53.190 50.493 1.00 27.58 1DLC4882 HETATM 4759 O HOH 61 41.276 73.788 36.658 1.00 32.95 1DLC4883 HETATM 4760 O HOH 62 47.841 44.305 49.214 1.00 32.69 1DLC4884 HETATM 4761 O HOH 63 35.489 33.715 61.967 1.00 28.50 1DLC4885 HETATM 4762 O HOH 64 56.538 77.886 37.982 1.00 50.68 1DLC4886 HETATM 4763 O HOH 65 18.717 10.880 30.116 1.00 45.47 1DLC4887 HETATM 4764 O HOH 66 36.692 51.483 75.590 1.00 36.31 1DLC4888 HETATM 4765 O HOH 67 20.585 18.690 41.004 1.00 34.39 1DLC4889 HETATM 4766 O HOH 68 40.508 40.198 41.474 1.00 39.41 1DLC4890 HETATM 4767 O HOH 69 39.908 45.560 74.947 1.00 33.34 1DLC4891 HETATM 4768 O HOH 70 14.617 25.579 48.494 1.00 25.51 1DLC4892 HETATM 4769 O HOH 71 46.860 64.590 54.372 1.00 34.61 1DLC4893 HETATM 4770 O HOH 72 38.042 46.135 38.081 1.00 30.46 1DLC4894 HETATM 4771 O HOH 73 14.223 18.604 37.526 1.00 33.61 1DLC4895 HETATM 4772 O HOH 74 41.396 33.509 59.099 1.00 33.96 1DLC4896 HETATM 4773 O HOH 75 36.159 56.059 54.037 1.00 29.86 1DLC4897 HETATM 4774 O HOH 76 25.313 32.849 50.116 1.00 32.15 1DLC4898 HETATM 4775 O HOH 77 11.778 10.641 30.101 1.00 44.03 1DLC4899 HETATM 4776 O HOH 78 42.893 28.299 64.966 1.00 47.47 1DLC4900 HETATM 4777 O HOH 79 46.675 54.242 75.812 1.00 38.86 1DLC4901 HETATM 4778 O HOH 80 45.755 41.679 55.898 1.00 34.63 1DLC4902 HETATM 4779 O HOH 81 25.484 44.446 46.854 1.00 35.35 1DLC4903 HETATM 4780 O HOH 82 15.402 8.669 44.437 1.00 51.05 1DLC4904 HETATM 4781 O HOH 83 29.189 60.967 26.317 1.00 41.92 1DLC4905 HETATM 4782 O HOH 84 28.869 40.731 48.778 1.00 51.15 1DLC4906 HETATM 4783 O HOH 85 45.082 38.563 44.823 1.00 33.55 1DLC4907 HETATM 4784 O HOH 86 1.705 23.575 29.683 1.00 48.74 1DLC4908 HETATM 4785 O HOH 87 27.621 39.569 70.673 1.00 40.98 1DLC4909 HETATM 4786 O HOH 88 26.008 29.161 48.418 1.00 29.63 1DLC4910 HETATM 4787 O HOH 89 25.317 11.429 47.522 1.00 27.37 1DLC4911 HETATM 4788O HOH 90 30.222 33.188 52.083 1.00 37.13 1DLC4912 HETATM 4789 O HOH 91 38.198 20.113 36.178 1.00 61.28 1DLC4913 HETATM 4790 O HOH 92 36.499 29.557 39.290 1.00 29.56 1DLC4914 HETATM 4791 O HOH 93 19.705 36.665 52.735 1.00 35.61 1DLC4915 HETATM 4792 O HOH 94 26.886 41.897 52.319 1.00 48.74 1DLC4916 HETATM 4793 O HOH 95 44.038 20.253 40.363 1.00 39.20 1DLC4917 HETATM 4794 O HOH 96 31.519 47.240 51.443 1.00 28.48 1DLC4918 HETATM 4795 O HOH 97 29.028 35.445 61.838 1.00 35.57 1DLC4919 HETATM 4796 O HOH 98 14.327 29.302 33.611 1.00 41.11 1DLC4920 HETATM 4797 O HOH 99 19.576 61.182 35.587 1.00 45.66 1DLC4921 HETATM 4798O HOH 100 56.227 72.862 32.221 1.00 54.49 1DLC4922 HETATM 4799 O HOH 101 15.572 41.260 36.469 1.00 34.12 1DLC4923 HETATM 4800 O HOH 102 46.292 25.845 33.724 1.00 52.88 1DLC4924 HETATM 4801 O HOH 103 32.306 63.512 40.031 1.00 53.52 1DLC4925 HETATM 4802 O HOH 104 34.104 44.558 47.227 1.00 32.41 1DLC4926 HETATM 4803 O HOH 105 44.964 39.206 57.270 1.00 43.16 1DLC4927 HETATM 4804 O HOH 106 56.545 54.651 60.410 1.00 56.15 1DLC4928 MASTER 63 2 0 0 0 0 0 6 4803 1 0 45 1DLC4929 END 1DLC4930 1DLC4930 __________________________________________________________________________
All of the compositions and methods disclosed and claimed herein can be made and executed without undue experimentation in light of the present disclosure. While the compositions and methods of this invention have been described in terms of preferred embodiments, it will be apparent to those of skill in the art that variations may be applied to the compositions and methods and in the steps or in the sequence of steps of the method described herein without departing from the concept, spirit and scope of the invention. More specifically, it will be apparent that certain agents which are both chemically and physiologically related may be substituted for the agents described herein while the same or similar results would be achieved. All such similar substitutes and modifications apparent to those skilled in the art are deemed to be within the spirit, scope and concept of the invention as defined by the appended claims.
__________________________________________________________________________
# SEQUENCE LISTING
- (1) GENERAL INFORMATION:
- (iii) NUMBER OF SEQUENCES: 113
- (2) INFORMATION FOR SEQ ID NO:1:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:1:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA TTT CA - #C CAT TCT CGT CGT TCT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Phe Hi - #s His Ser Arg Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:2:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:2:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Phe Hi - #s His Ser Arg Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:3:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:3:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTC CTT AGT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Leu Ser Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:4:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:4:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Leu Ser Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:5:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:5:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT CCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Pro Glu
# 220
- GAT GTT GCT GAA TTC AGT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Ser His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:6:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:6:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Pro Glu
# 220
- Asp Val Ala Glu Phe Ser His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:7:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:7:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTC TAT CGT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:8:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:8:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:9:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:9:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTC TAT AAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr Asn Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- TCT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Ser Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:10:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:10:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr Asn Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Ser Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:11:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:11:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTC TAT ACC AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr Thr Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:12:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:12:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr Thr Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:13:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:13:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT AAT TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Asn Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:14:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:14:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Asn Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:15:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:15:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TTA CTT ACT ACG CT - #T CAG AAG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Leu Leu Thr Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:16:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:16:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Leu Leu Thr Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:17:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:17:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT ACC CTT AAT ACA CT - #A CAG AAG TGC GGA CCA
960
Phe Thr Asp Pro Ile Phe Thr Leu Asn Thr Le - #u Gln Lys Cys Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:18:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:18:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Thr Leu Asn Thr Le - #u Gln Lys Cys Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:19:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:19:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT GCC GTT AAT ACT CT - #G TGG GAA TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Ala Val Asn Thr Le - #u Trp Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:20:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:20:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ala Val Asn Thr Le - #u Trp Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:21:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:21:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTC TAT CGT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TTA CTT ACT ACG CT - #T CAG AAG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Leu Leu Thr Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:22:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:22:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Leu Leu Thr Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:23:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:23:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT ACG CCA ACC ACC CT - #A CAG GAT TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Thr Pro Thr Thr Le - #u Gln Asp Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:24:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:24:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Thr Pro Thr Thr Le - #u Gln Asp Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:25:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:25:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT GCC CTG AAT ACC TT - #A GAC GAG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Ala Leu Asn Thr Le - #u Asp Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:26:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:26:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ala Leu Asn Thr Le - #u Asp Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:27:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:27:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAC GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ACT AGG CGA TTC AGA AAG GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Thr Arg Arg Phe Arg Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:28:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:28:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Thr Arg Arg Phe Arg Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:29:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:29:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTC TAT CGT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TTA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Leu Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:30:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:30:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Leu Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:31:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:31:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT ATC CTC AAT ACG CT - #A CAG GAG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Ile Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:32:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:32:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ile Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:33:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:33:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT ATC CTA CAT ACG CT - #G CAG GAG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Ile Leu His Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:34:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:34:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ile Leu His Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:35:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:35:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCC CTC GTT AAC CT - #A ATG GTG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Val Asn Le - #u Met Val Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:36:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:36:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Val Asn Le - #u Met Val Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:37:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:37:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCT CTT AGG ACA CC - #A CTT GCG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Arg Thr Pr - #o Leu Ala Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:38:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:38:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Arg Thr Pr - #o Leu Ala Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:39:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:39:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TTC AAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Phe Asn
# 285
- ATT TTG CTT TAC AGT AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Leu Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:40:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:40:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Phe Asn
# 285
- Ile Leu Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:41:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:41:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT GTG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Val Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:42:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:42:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Val Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:43:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:43:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GGT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:44:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:44:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:45:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:45:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AAT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Asn
145 1 - #50 1 - #55 1 -
#60
- CCA CAC AGC CAA GGT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Pro His Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:46:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:46:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Asn
145 1 - #50 1 - #55 1 -
#60
- Pro His Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:47:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:47:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- GTT CGG TTA TAC CCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:48:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:48:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:49:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:49:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AAT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Asn
145 1 - #50 1 - #55 1 -
#60
- CCA CAC AGC CAA GGT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Pro His Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- GTT CGG TTA TAC CCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:50:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:50:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Asn
145 1 - #50 1 - #55 1 -
#60
- Pro His Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:51:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1956 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1953
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:51:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAA GAC CCA TGG AA - #G GCT TTT ATG GCA CAA
336
Asn Thr Ile Trp Pro Ser Glu Asp Pro Trp Ly - #s Ala Phe Met Ala Gln
# 110
- GTT GAA GTA CTG ATA GAT AAG AAA ATA GAG GA - #G TAT GCT AAA AGT AAA
384
Val Glu Val Leu Ile Asp Lys Lys Ile Glu Gl - #u Tyr Ala Lys Ser Lys
# 125
- GCT CTT GCA GAG TTA CAG GGT CTT CAA AAT AA - #T TTC GAA GAT TAT GTT
432
Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn As - #n Phe Glu Asp Tyr Val
# 140
- AAT GCG TTA AAT TCC TGG AAG AAA ACA CCT TT - #A AGT TTG CGA AGT AAA
480
Asn Ala Leu Asn Ser Trp Lys Lys Thr Pro Le - #u Ser Leu Arg Ser Lys
145 1 - #50 1 - #55 1 -
#60
- AGA AGC CAA GAT CGA ATA AGG GAA CTT TTT TC - #T CAA GCA GAA AGT CAT
528
Arg Ser Gln Asp Arg Ile Arg Glu Leu Phe Se - #r Gln Ala Glu Ser His
# 175
- TTT CGT AAT TCC ATG CCG TCA TTT GCA GTT TC - #C AAA TTC GAA GTG CTG
576
Phe Arg Asn Ser Met Pro Ser Phe Ala Val Se - #r Lys Phe Glu Val Leu
# 190
- TTT CTA CCA ACA TAT GCA CAA GCT GCA AAT AC - #A CAT TTA TTG CTA TTA
624
Phe Leu Pro Thr Tyr Ala Gln Ala Ala Asn Th - #r His Leu Leu Leu Leu
# 205
- AAA GAT GCT CAA GTT TTT GGA GAA GAA TGG GG - #A TAT TCT TCA GAA GAT
672
Lys Asp Ala Gln Val Phe Gly Glu Glu Trp Gl - #y Tyr Ser Ser Glu Asp
# 220
- GTT GCT GAA TTT TAT CAT AGA CAA TTA AAA CT - #T ACA CAA CAA TAC ACT
720
Val Ala Glu Phe Tyr His Arg Gln Leu Lys Le - #u Thr Gln Gln Tyr Thr
225 2 - #30 2 - #35 2 -
#40
- GAC CAT TGT GTT AAT TGG TAT AAT GTT GGA TT - #A AAT GGT TTA AGA GGT
768
Asp His Cys Val Asn Trp Tyr Asn Val Gly Le - #u Asn Gly Leu Arg Gly
# 255
- TCA ACT TAT GAT GCA TGG GTC AAA TTT AAC CG - #T TTT CGC AGA GAA ATG
816
Ser Thr Tyr Asp Ala Trp Val Lys Phe Asn Ar - #g Phe Arg Arg Glu Met
# 270
- ACT TTA ACT GTA TTA GAT CTA ATT GTA CTT TT - #C CCA TTT TAT GAT ATT
864
Thr Leu Thr Val Leu Asp Leu Ile Val Leu Ph - #e Pro Phe Tyr Asp Ile
# 285
- CGG TTA TAC TCA AAA GGG GTT AAA ACA GAA CT - #A ACA AGA GAC ATT TTT
912
Arg Leu Tyr Ser Lys Gly Val Lys Thr Glu Le - #u Thr Arg Asp Ile Phe
# 300
- ACG GAT CCA ATT TTT TCA CTT AAT ACT CTT CA - #G GAG TAT GGA CCA ACT
960
Thr Asp Pro Ile Phe Ser Leu Asn Thr Leu Gl - #n Glu Tyr Gly Pro Thr
305 3 - #10 3 - #15 3 -
#20
- TTT TTG AGT ATA GAA AAC TCT ATT CGA AAA CC - #T CAT TTA TTT GAT TAT
1008
Phe Leu Ser Ile Glu Asn Ser Ile Arg Lys Pr - #o His Leu Phe Asp Tyr
# 335
- TTA CAG GGG ATT GAA TTT CAT ACG CGT CTT CA - #A CCT GGT TAC TTT GGG
1056
Leu Gln Gly Ile Glu Phe His Thr Arg Leu Gl - #n Pro Gly Tyr Phe Gly
# 350
- AAA GAT TCT TTC AAT TAT TGG TCT GGT AAT TA - #T GTA GAA ACT AGA CCT
1104
Lys Asp Ser Phe Asn Tyr Trp Ser Gly Asn Ty - #r Val Glu Thr Arg Pro
# 365
- AGT ATA GGA TCT AGT AAG ACA ATT ACT TCC CC - #A TTT TAT GGA GAT AAA
1152
Ser Ile Gly Ser Ser Lys Thr Ile Thr Ser Pr - #o Phe Tyr Gly Asp Lys
# 380
- TCT ACT GAA CCT GTA CAA AAG CTA AGC TTT GA - #T GGA CAA AAA GTT TAT
1200
Ser Thr Glu Pro Val Gln Lys Leu Ser Phe As - #p Gly Gln Lys Val Tyr
385 3 - #90 3 - #95 4 -
#00
- CGA ACT ATA GCT AAT ACA GAC GTA GCG GCT TG - #G CCG AAT GGT AAG GTA
1248
Arg Thr Ile Ala Asn Thr Asp Val Ala Ala Tr - #p Pro Asn Gly Lys Val
# 415
- TAT TTA GGT GTT ACG AAA GTT GAT TTT AGT CA - #A TAT GAT GAT CAA AAA
1296
Tyr Leu Gly Val Thr Lys Val Asp Phe Ser Gl - #n Tyr Asp Asp Gln Lys
# 430
- AAT GAA ACT AGT ACA CAA ACA TAT GAT TCA AA - #A AGA AAC AAT GGC CAT
1344
Asn Glu Thr Ser Thr Gln Thr Tyr Asp Ser Ly - #s Arg Asn Asn Gly His
# 445
- GTA AGT GCA CAG GAT TCT ATT GAC CAA TTA CC - #G CCA GAA ACA ACA GAT
1392
Val Ser Ala Gln Asp Ser Ile Asp Gln Leu Pr - #o Pro Glu Thr Thr Asp
# 460
- GAA CCA CTT GAA AAA GCA TAT AGT CAT CAG CT - #T AAT TAC GCG GAA TGT
1440
Glu Pro Leu Glu Lys Ala Tyr Ser His Gln Le - #u Asn Tyr Ala Glu Cys
465 4 - #70 4 - #75 4 -
#80
- TTC TTA ATG CAG GAC CGT CGT GGA ACA ATT CC - #A TTT TTT ACT TGG ACA
1488
Phe Leu Met Gln Asp Arg Arg Gly Thr Ile Pr - #o Phe Phe Thr Trp Thr
# 495
- CAT AGA AGT GTA GAC TTT TTT AAT ACA ATT GA - #T GCT GAA AAG ATT ACT
1536
His Arg Ser Val Asp Phe Phe Asn Thr Ile As - #p Ala Glu Lys Ile Thr
# 510
- CAA CTT CCA GTA GTG AAA GCA TAT GCC TTG TC - #T TCA GGT GCT TCC ATT
1584
Gln Leu Pro Val Val Lys Ala Tyr Ala Leu Se - #r Ser Gly Ala Ser Ile
# 525
- ATT GAA GGT CCA GGA TTC ACA GGA GGA AAT TT - #A CTA TTC CTA AAA GAA
1632
Ile Glu Gly Pro Gly Phe Thr Gly Gly Asn Le - #u Leu Phe Leu Lys Glu
# 540
- TCT AGT AAT TCA ATT GCT AAA TTT AAA GTT AC - #A TTA AAT TCA GCA GCC
1680
Ser Ser Asn Ser Ile Ala Lys Phe Lys Val Th - #r Leu Asn Ser Ala Ala
545 5 - #50 5 - #55 5 -
#60
- TTG TTA CAA CGA TAT CGT GTA AGA ATA CGC TA - #T GCT TCT ACC ACT AAC
1728
Leu Leu Gln Arg Tyr Arg Val Arg Ile Arg Ty - #r Ala Ser Thr Thr Asn
# 575
- TTA CGA CTT TTT GTG CAA AAT TCA AAC AAT GA - #T TTT CTT GTC ATC TAC
1776
Leu Arg Leu Phe Val Gln Asn Ser Asn Asn As - #p Phe Leu Val Ile Tyr
# 590
- ATT AAT AAA ACT ATG AAT AAA GAT GAT GAT TT - #A ACA TAT CAA ACA TTT
1824
Ile Asn Lys Thr Met Asn Lys Asp Asp Asp Le - #u Thr Tyr Gln Thr Phe
# 605
- GAT CTC GCA ACT ACT AAT TCT AAT ATG GGG TT - #C TCG GGT GAT AAG AAT
1872
Asp Leu Ala Thr Thr Asn Ser Asn Met Gly Ph - #e Ser Gly Asp Lys Asn
# 620
- GAA CTT ATA ATA GGA GCA GAA TCT TTC GTT TC - #T AAT GAA AAA ATC TAT
1920
Glu Leu Ile Ile Gly Ala Glu Ser Phe Val Se - #r Asn Glu Lys Ile Tyr
625 6 - #30 6 - #35 6 -
#40
# 1956AAG ATA GAA TTT ATC CCA GTA CAA TT - #G TAA
Ile Asp Lys Ile Glu Phe Ile Pro Val Gln Le - #u
# 650
- (2) INFORMATION FOR SEQ ID NO:52:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 651 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:52:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Glu Asp Pro Trp Ly - #s Ala Phe Met Ala Gln
# 110
- Val Glu Val Leu Ile Asp Lys Lys Ile Glu Gl - #u Tyr Ala Lys Ser Lys
# 125
- Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn As - #n Phe Glu Asp Tyr Val
# 140
- Asn Ala Leu Asn Ser Trp Lys Lys Thr Pro Le - #u Ser Leu Arg Ser Lys
145 1 - #50 1 - #55 1 -
#60
- Arg Ser Gln Asp Arg Ile Arg Glu Leu Phe Se - #r Gln Ala Glu Ser His
# 175
- Phe Arg Asn Ser Met Pro Ser Phe Ala Val Se - #r Lys Phe Glu Val Leu
# 190
- Phe Leu Pro Thr Tyr Ala Gln Ala Ala Asn Th - #r His Leu Leu Leu Leu
# 205
- Lys Asp Ala Gln Val Phe Gly Glu Glu Trp Gl - #y Tyr Ser Ser Glu Asp
# 220
- Val Ala Glu Phe Tyr His Arg Gln Leu Lys Le - #u Thr Gln Gln Tyr Thr
225 2 - #30 2 - #35 2 -
#40
- Asp His Cys Val Asn Trp Tyr Asn Val Gly Le - #u Asn Gly Leu Arg Gly
# 255
- Ser Thr Tyr Asp Ala Trp Val Lys Phe Asn Ar - #g Phe Arg Arg Glu Met
# 270
- Thr Leu Thr Val Leu Asp Leu Ile Val Leu Ph - #e Pro Phe Tyr Asp Ile
# 285
- Arg Leu Tyr Ser Lys Gly Val Lys Thr Glu Le - #u Thr Arg Asp Ile Phe
# 300
- Thr Asp Pro Ile Phe Ser Leu Asn Thr Leu Gl - #n Glu Tyr Gly Pro Thr
305 3 - #10 3 - #15 3 -
#20
- Phe Leu Ser Ile Glu Asn Ser Ile Arg Lys Pr - #o His Leu Phe Asp Tyr
# 335
- Leu Gln Gly Ile Glu Phe His Thr Arg Leu Gl - #n Pro Gly Tyr Phe Gly
# 350
- Lys Asp Ser Phe Asn Tyr Trp Ser Gly Asn Ty - #r Val Glu Thr Arg Pro
# 365
- Ser Ile Gly Ser Ser Lys Thr Ile Thr Ser Pr - #o Phe Tyr Gly Asp Lys
# 380
- Ser Thr Glu Pro Val Gln Lys Leu Ser Phe As - #p Gly Gln Lys Val Tyr
385 3 - #90 3 - #95 4 -
#00
- Arg Thr Ile Ala Asn Thr Asp Val Ala Ala Tr - #p Pro Asn Gly Lys Val
# 415
- Tyr Leu Gly Val Thr Lys Val Asp Phe Ser Gl - #n Tyr Asp Asp Gln Lys
# 430
- Asn Glu Thr Ser Thr Gln Thr Tyr Asp Ser Ly - #s Arg Asn Asn Gly His
# 445
- Val Ser Ala Gln Asp Ser Ile Asp Gln Leu Pr - #o Pro Glu Thr Thr Asp
# 460
- Glu Pro Leu Glu Lys Ala Tyr Ser His Gln Le - #u Asn Tyr Ala Glu Cys
465 4 - #70 4 - #75 4 -
#80
- Phe Leu Met Gln Asp Arg Arg Gly Thr Ile Pr - #o Phe Phe Thr Trp Thr
# 495
- His Arg Ser Val Asp Phe Phe Asn Thr Ile As - #p Ala Glu Lys Ile Thr
# 510
- Gln Leu Pro Val Val Lys Ala Tyr Ala Leu Se - #r Ser Gly Ala Ser Ile
# 525
- Ile Glu Gly Pro Gly Phe Thr Gly Gly Asn Le - #u Leu Phe Leu Lys Glu
# 540
- Ser Ser Asn Ser Ile Ala Lys Phe Lys Val Th - #r Leu Asn Ser Ala Ala
545 5 - #50 5 - #55 5 -
#60
- Leu Leu Gln Arg Tyr Arg Val Arg Ile Arg Ty - #r Ala Ser Thr Thr Asn
# 575
- Leu Arg Leu Phe Val Gln Asn Ser Asn Asn As - #p Phe Leu Val Ile Tyr
# 590
- Ile Asn Lys Thr Met Asn Lys Asp Asp Asp Le - #u Thr Tyr Gln Thr Phe
# 605
- Asp Leu Ala Thr Thr Asn Ser Asn Met Gly Ph - #e Ser Gly Asp Lys Asn
# 620
- Glu Leu Ile Ile Gly Ala Glu Ser Phe Val Se - #r Asn Glu Lys Ile Tyr
625 6 - #30 6 - #35 6 -
#40
- Ile Asp Lys Ile Glu Phe Ile Pro Val Gln Le - #u
# 650
- (2) INFORMATION FOR SEQ ID NO:53:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:53:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC GGA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Gly Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:54:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:54:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Gly Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:55:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1956 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1953
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:55:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAA GAC CCA TGG AA - #G GCT TTT ATG GCA CAA
336
Asn Thr Ile Trp Pro Ser Glu Asp Pro Trp Ly - #s Ala Phe Met Ala Gln
# 110
- GTT GAA GTA CTG ATA GAT AAG AAA ATA GAG GA - #G TAT GCT AAA AGT AAA
384
Val Glu Val Leu Ile Asp Lys Lys Ile Glu Gl - #u Tyr Ala Lys Ser Lys
# 125
- GCT CTT GCA GAG TTA CAG GGT CTT CAA AAT AA - #T TTC GAA GAT TAT GTT
432
Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn As - #n Phe Glu Asp Tyr Val
# 140
- AAT GCG TTA AAT TCC TGG AAG AAA ACA CCT TT - #A AGT TTG CGA AAT CCA
480
Asn Ala Leu Asn Ser Trp Lys Lys Thr Pro Le - #u Ser Leu Arg Asn Pro
145 1 - #50 1 - #55 1 -
#60
- CAC AGC CAA GGT CGA ATA AGG GAA CTT TTT TC - #T CAA GCA GAA AGT CAT
528
His Ser Gln Gly Arg Ile Arg Glu Leu Phe Se - #r Gln Ala Glu Ser His
# 175
- TTT CGT AAT TCC ATG CCG TCA TTT GCA GTT TC - #C AAA TTC GAA GTG CTG
576
Phe Arg Asn Ser Met Pro Ser Phe Ala Val Se - #r Lys Phe Glu Val Leu
# 190
- TTT CTA CCA ACA TAT GCA CAA GCT GCA AAT AC - #A CAT TTA TTG CTA TTA
624
Phe Leu Pro Thr Tyr Ala Gln Ala Ala Asn Th - #r His Leu Leu Leu Leu
# 205
- AAA GAT GCT CAA GTT TTT GGA GAA GAA TGG GG - #A TAT TCT TCA GAA GAT
672
Lys Asp Ala Gln Val Phe Gly Glu Glu Trp Gl - #y Tyr Ser Ser Glu Asp
# 220
- GTT GCT GAA TTT TAT CAT AGA CAA TTA AAA CT - #T ACA CAA CAA TAC ACT
720
Val Ala Glu Phe Tyr His Arg Gln Leu Lys Le - #u Thr Gln Gln Tyr Thr
225 2 - #30 2 - #35 2 -
#40
- GAC CAT TGT GTT AAT TGG TAT AAT GTT GGA TT - #A AAT GGT TTA AGA GGT
768
Asp His Cys Val Asn Trp Tyr Asn Val Gly Le - #u Asn Gly Leu Arg Gly
# 255
- TCA ACT TAT GAT GCA TGG GTC AAA TTT AAC CG - #T TTT CGC AGA GAA ATG
816
Ser Thr Tyr Asp Ala Trp Val Lys Phe Asn Ar - #g Phe Arg Arg Glu Met
# 270
- ACT TTA ACT GTA TTA GAT CTA ATT GTA CTT TT - #C CCA TTT TAT GAT ATT
864
Thr Leu Thr Val Leu Asp Leu Ile Val Leu Ph - #e Pro Phe Tyr Asp Ile
# 285
- CGG TTA TAC TCA AAA GGG GTT AAA ACA GAA CT - #A ACA AGA GAC ATT TTT
912
Arg Leu Tyr Ser Lys Gly Val Lys Thr Glu Le - #u Thr Arg Asp Ile Phe
# 300
- ACG GAT CCA ATT TTT TCA CTT AAT ACT CTT CA - #G GAG TAT GGA CCA ACT
960
Thr Asp Pro Ile Phe Ser Leu Asn Thr Leu Gl - #n Glu Tyr Gly Pro Thr
305 3 - #10 3 - #15 3 -
#20
- TTT TTG AGT ATA GAA AAC TCT ATT CGA AAA CC - #T CAT TTA TTT GAT TAT
1008
Phe Leu Ser Ile Glu Asn Ser Ile Arg Lys Pr - #o His Leu Phe Asp Tyr
# 335
- TTA CAG GGG ATT GAA TTT CAT ACG CGT CTT CA - #A CCT GGT TAC TTT GGG
1056
Leu Gln Gly Ile Glu Phe His Thr Arg Leu Gl - #n Pro Gly Tyr Phe Gly
# 350
- AAA GAT TCT TTC AAT TAT TGG TCT GGT AAT TA - #T GTA GAA ACT AGA CCT
1104
Lys Asp Ser Phe Asn Tyr Trp Ser Gly Asn Ty - #r Val Glu Thr Arg Pro
# 365
- AGT ATA GGA TCT AGT AAG ACA ATT ACT TCC CC - #A TTT TAT GGA GAT AAA
1152
Ser Ile Gly Ser Ser Lys Thr Ile Thr Ser Pr - #o Phe Tyr Gly Asp Lys
# 380
- TCT ACT GAA CCT GTA CAA AAG CTA AGC TTT GA - #T GGA CAA AAA GTT TAT
1200
Ser Thr Glu Pro Val Gln Lys Leu Ser Phe As - #p Gly Gln Lys Val Tyr
385 3 - #90 3 - #95 4 -
#00
- CGA ACT ATA GCT AAT ACA GAC GTA GCG GCT TG - #G CCG AAT GGT AAG GTA
1248
Arg Thr Ile Ala Asn Thr Asp Val Ala Ala Tr - #p Pro Asn Gly Lys Val
# 415
- TAT TTA GGT GTT ACG AAA GTT GAT TTT AGT CA - #A TAT GAT GAT CAA AAA
1296
Tyr Leu Gly Val Thr Lys Val Asp Phe Ser Gl - #n Tyr Asp Asp Gln Lys
# 430
- AAT GAA ACT AGT ACA CAA ACA TAT GAT TCA AA - #A AGA AAC AAT GGC CAT
1344
Asn Glu Thr Ser Thr Gln Thr Tyr Asp Ser Ly - #s Arg Asn Asn Gly His
# 445
- GTA AGT GCA CAG GAT TCT ATT GAC CAA TTA CC - #G CCA GAA ACA ACA GAT
1392
Val Ser Ala Gln Asp Ser Ile Asp Gln Leu Pr - #o Pro Glu Thr Thr Asp
# 460
- GAA CCA CTT GAA AAA GCA TAT AGT CAT CAG CT - #T AAT TAC GCG GAA TGT
1440
Glu Pro Leu Glu Lys Ala Tyr Ser His Gln Le - #u Asn Tyr Ala Glu Cys
465 4 - #70 4 - #75 4 -
#80
- TTC TTA ATG CAG GAC CGT CGT GGA ACA ATT CC - #A TTT TTT ACT TGG ACA
1488
Phe Leu Met Gln Asp Arg Arg Gly Thr Ile Pr - #o Phe Phe Thr Trp Thr
# 495
- CAT AGA AGT GTA GAC TTT TTT AAT ACA ATT GA - #T GCT GAA AAG ATT ACT
1536
His Arg Ser Val Asp Phe Phe Asn Thr Ile As - #p Ala Glu Lys Ile Thr
# 510
- CAA CTT CCA GTA GTG AAA GCA TAT GCC TTG TC - #T TCA GGT GCT TCC ATT
1584
Gln Leu Pro Val Val Lys Ala Tyr Ala Leu Se - #r Ser Gly Ala Ser Ile
# 525
- ATT GAA GGT CCA GGA TTC ACA GGA GGA AAT TT - #A CTA TTC CTA AAA GAA
1632
Ile Glu Gly Pro Gly Phe Thr Gly Gly Asn Le - #u Leu Phe Leu Lys Glu
# 540
- TCT AGT AAT TCA ATT GCT AAA TTT AAA GTT AC - #A TTA AAT TCA GCA GCC
1680
Ser Ser Asn Ser Ile Ala Lys Phe Lys Val Th - #r Leu Asn Ser Ala Ala
545 5 - #50 5 - #55 5 -
#60
- TTG TTA CAA CGA TAT CGT GTA AGA ATA CGC TA - #T GCT TCT ACC ACT AAC
1728
Leu Leu Gln Arg Tyr Arg Val Arg Ile Arg Ty - #r Ala Ser Thr Thr Asn
# 575
- TTA CGA CTT TTT GTG CAA AAT TCA AAC AAT GA - #T TTT CTT GTC ATC TAC
1776
Leu Arg Leu Phe Val Gln Asn Ser Asn Asn As - #p Phe Leu Val Ile Tyr
# 590
- ATT AAT AAA ACT ATG AAT AAA GAT GAT GAT TT - #A ACA TAT CAA ACA TTT
1824
Ile Asn Lys Thr Met Asn Lys Asp Asp Asp Le - #u Thr Tyr Gln Thr Phe
# 605
- GAT CTC GCA ACT ACT AAT TCT AAT ATG GGG TT - #C TCG GGT GAT AAG AAT
1872
Asp Leu Ala Thr Thr Asn Ser Asn Met Gly Ph - #e Ser Gly Asp Lys Asn
# 620
- GAA CTT ATA ATA GGA GCA GAA TCT TTC GTT TC - #T AAT GAA AAA ATC TAT
1920
Glu Leu Ile Ile Gly Ala Glu Ser Phe Val Se - #r Asn Glu Lys Ile Tyr
625 6 - #30 6 - #35 6 -
#40
# 1956AAG ATA GAA TTT ATC CCA GTA CAA TT - #G TAA
Ile Asp Lys Ile Glu Phe Ile Pro Val Gln Le - #u
# 650
- (2) INFORMATION FOR SEQ ID NO:56:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 651 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:56:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Glu Asp Pro Trp Ly - #s Ala Phe Met Ala Gln
# 110
- Val Glu Val Leu Ile Asp Lys Lys Ile Glu Gl - #u Tyr Ala Lys Ser Lys
# 125
- Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn As - #n Phe Glu Asp Tyr Val
# 140
- Asn Ala Leu Asn Ser Trp Lys Lys Thr Pro Le - #u Ser Leu Arg Asn Pro
145 1 - #50 1 - #55 1 -
#60
- His Ser Gln Gly Arg Ile Arg Glu Leu Phe Se - #r Gln Ala Glu Ser His
# 175
- Phe Arg Asn Ser Met Pro Ser Phe Ala Val Se - #r Lys Phe Glu Val Leu
# 190
- Phe Leu Pro Thr Tyr Ala Gln Ala Ala Asn Th - #r His Leu Leu Leu Leu
# 205
- Lys Asp Ala Gln Val Phe Gly Glu Glu Trp Gl - #y Tyr Ser Ser Glu Asp
# 220
- Val Ala Glu Phe Tyr His Arg Gln Leu Lys Le - #u Thr Gln Gln Tyr Thr
225 2 - #30 2 - #35 2 -
#40
- Asp His Cys Val Asn Trp Tyr Asn Val Gly Le - #u Asn Gly Leu Arg Gly
# 255
- Ser Thr Tyr Asp Ala Trp Val Lys Phe Asn Ar - #g Phe Arg Arg Glu Met
# 270
- Thr Leu Thr Val Leu Asp Leu Ile Val Leu Ph - #e Pro Phe Tyr Asp Ile
# 285
- Arg Leu Tyr Ser Lys Gly Val Lys Thr Glu Le - #u Thr Arg Asp Ile Phe
# 300
- Thr Asp Pro Ile Phe Ser Leu Asn Thr Leu Gl - #n Glu Tyr Gly Pro Thr
305 3 - #10 3 - #15 3 -
#20
- Phe Leu Ser Ile Glu Asn Ser Ile Arg Lys Pr - #o His Leu Phe Asp Tyr
# 335
- Leu Gln Gly Ile Glu Phe His Thr Arg Leu Gl - #n Pro Gly Tyr Phe Gly
# 350
- Lys Asp Ser Phe Asn Tyr Trp Ser Gly Asn Ty - #r Val Glu Thr Arg Pro
# 365
- Ser Ile Gly Ser Ser Lys Thr Ile Thr Ser Pr - #o Phe Tyr Gly Asp Lys
# 380
- Ser Thr Glu Pro Val Gln Lys Leu Ser Phe As - #p Gly Gln Lys Val Tyr
385 3 - #90 3 - #95 4 -
#00
- Arg Thr Ile Ala Asn Thr Asp Val Ala Ala Tr - #p Pro Asn Gly Lys Val
# 415
- Tyr Leu Gly Val Thr Lys Val Asp Phe Ser Gl - #n Tyr Asp Asp Gln Lys
# 430
- Asn Glu Thr Ser Thr Gln Thr Tyr Asp Ser Ly - #s Arg Asn Asn Gly His
# 445
- Val Ser Ala Gln Asp Ser Ile Asp Gln Leu Pr - #o Pro Glu Thr Thr Asp
# 460
- Glu Pro Leu Glu Lys Ala Tyr Ser His Gln Le - #u Asn Tyr Ala Glu Cys
465 4 - #70 4 - #75 4 -
#80
- Phe Leu Met Gln Asp Arg Arg Gly Thr Ile Pr - #o Phe Phe Thr Trp Thr
# 495
- His Arg Ser Val Asp Phe Phe Asn Thr Ile As - #p Ala Glu Lys Ile Thr
# 510
- Gln Leu Pro Val Val Lys Ala Tyr Ala Leu Se - #r Ser Gly Ala Ser Ile
# 525
- Ile Glu Gly Pro Gly Phe Thr Gly Gly Asn Le - #u Leu Phe Leu Lys Glu
# 540
- Ser Ser Asn Ser Ile Ala Lys Phe Lys Val Th - #r Leu Asn Ser Ala Ala
545 5 - #50 5 - #55 5 -
#60
- Leu Leu Gln Arg Tyr Arg Val Arg Ile Arg Ty - #r Ala Ser Thr Thr Asn
# 575
- Leu Arg Leu Phe Val Gln Asn Ser Asn Asn As - #p Phe Leu Val Ile Tyr
# 590
- Ile Asn Lys Thr Met Asn Lys Asp Asp Asp Le - #u Thr Tyr Gln Thr Phe
# 605
- Asp Leu Ala Thr Thr Asn Ser Asn Met Gly Ph - #e Ser Gly Asp Lys Asn
# 620
- Glu Leu Ile Ile Gly Ala Glu Ser Phe Val Se - #r Asn Glu Lys Ile Tyr
625 6 - #30 6 - #35 6 -
#40
- Ile Asp Lys Ile Glu Phe Ile Pro Val Gln Le - #u
# 650
- (2) INFORMATION FOR SEQ ID NO:57:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1956 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1953
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:57:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAA GAC CCA TGG AA - #G GCT TTT ATG GCA CAA
336
Asn Thr Ile Trp Pro Ser Glu Asp Pro Trp Ly - #s Ala Phe Met Ala Gln
# 110
- GTT GAA GTA CTG ATA GAT AAG AAA ATA GAG GA - #G TAT GCT AAA AGT AAA
384
Val Glu Val Leu Ile Asp Lys Lys Ile Glu Gl - #u Tyr Ala Lys Ser Lys
# 125
- GCT CTT GCA GAG TTA CAG GGT CTT CAA AAT AA - #T TTC GAA GAT TAT GTT
432
Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn As - #n Phe Glu Asp Tyr Val
# 140
- AAT GCG TTA AAT TCC TGG AAG AAA TTT CAC CA - #T TCT CGT CGT TCT AAA
480
Asn Ala Leu Asn Ser Trp Lys Lys Phe His Hi - #s Ser Arg Arg Ser Lys
145 1 - #50 1 - #55 1 -
#60
- AGA AGC CAA GAT CGA ATA AGG GAA CTT TTT TC - #T CAA GCA GAA AGT CAT
528
Arg Ser Gln Asp Arg Ile Arg Glu Leu Phe Se - #r Gln Ala Glu Ser His
# 175
- TTT CGT AAT TCC ATG CCG TCA TTT GCA GTT TC - #C AAA TTC GAA GTG CTG
576
Phe Arg Asn Ser Met Pro Ser Phe Ala Val Se - #r Lys Phe Glu Val Leu
# 190
- TTT CTA CCA ACA TAT GCA CAA GCT GCA AAT AC - #A CAT TTA TTG CTA TTA
624
Phe Leu Pro Thr Tyr Ala Gln Ala Ala Asn Th - #r His Leu Leu Leu Leu
# 205
- AAA GAT GCT CAA GTT TTT GGA GAA GAA TGG GG - #A TAT TCT TCA GAA GAT
672
Lys Asp Ala Gln Val Phe Gly Glu Glu Trp Gl - #y Tyr Ser Ser Glu Asp
# 220
- GTT GCT GAA TTT TAT CAT AGA CAA TTA AAA CT - #T ACA CAA CAA TAC ACT
720
Val Ala Glu Phe Tyr His Arg Gln Leu Lys Le - #u Thr Gln Gln Tyr Thr
225 2 - #30 2 - #35 2 -
#40
- GAC CAT TGT GTT AAT TGG TAT AAT GTT GGA TT - #A AAT GGT TTA AGA GGT
768
Asp His Cys Val Asn Trp Tyr Asn Val Gly Le - #u Asn Gly Leu Arg Gly
# 255
- TCA ACT TAT GAT GCA TGG GTC AAA TTT AAC CG - #T TTT CGC AGA GAA ATG
816
Ser Thr Tyr Asp Ala Trp Val Lys Phe Asn Ar - #g Phe Arg Arg Glu Met
# 270
- ACT TTA ACT GTA TTA GAT CTA ATT GTA CTT TT - #C CCA TTT TAT GAT ATT
864
Thr Leu Thr Val Leu Asp Leu Ile Val Leu Ph - #e Pro Phe Tyr Asp Ile
# 285
- CGG TTA TAC TCA AAA GGG GTT AAA ACA GAA CT - #A ACA AGA GAC ATT TTT
912
Arg Leu Tyr Ser Lys Gly Val Lys Thr Glu Le - #u Thr Arg Asp Ile Phe
# 300
- ACG GAT CCA ATT TTT TCA CTT AAT ACT CTT CA - #G GAG TAT GGA CCA ACT
960
Thr Asp Pro Ile Phe Ser Leu Asn Thr Leu Gl - #n Glu Tyr Gly Pro Thr
305 3 - #10 3 - #15 3 -
#20
- TTT TTG AGT ATA GAA AAC TCT ATT CGA AAA CC - #T CAT TTA TTT GAT TAT
1008
Phe Leu Ser Ile Glu Asn Ser Ile Arg Lys Pr - #o His Leu Phe Asp Tyr
# 335
- TTA CAG GGG ATT GAA TTT CAT ACG CGT CTT CA - #A CCT GGT TAC TTT GGG
1056
Leu Gln Gly Ile Glu Phe His Thr Arg Leu Gl - #n Pro Gly Tyr Phe Gly
# 350
- AAA GAT TCT TTC AAT TAT TGG TCT GGT AAT TA - #T GTA GAA ACT AGA CCT
1104
Lys Asp Ser Phe Asn Tyr Trp Ser Gly Asn Ty - #r Val Glu Thr Arg Pro
# 365
- AGT ATA GGA TCT AGT AAG ACA ATT ACT TCC CC - #A TTT TAT GGA GAT AAA
1152
Ser Ile Gly Ser Ser Lys Thr Ile Thr Ser Pr - #o Phe Tyr Gly Asp Lys
# 380
- TCT ACT GAA CCT GTA CAA AAG CTA AGC TTT GA - #T GGA CAA AAA GTT TAT
1200
Ser Thr Glu Pro Val Gln Lys Leu Ser Phe As - #p Gly Gln Lys Val Tyr
385 3 - #90 3 - #95 4 -
#00
- CGA ACT ATA GCT AAT ACA GAC GTA GCG GCT TG - #G CCG AAT GGT AAG GTA
1248
Arg Thr Ile Ala Asn Thr Asp Val Ala Ala Tr - #p Pro Asn Gly Lys Val
# 415
- TAT TTA GGT GTT ACG AAA GTT GAT TTT AGT CA - #A TAT GAT GAT CAA AAA
1296
Tyr Leu Gly Val Thr Lys Val Asp Phe Ser Gl - #n Tyr Asp Asp Gln Lys
# 430
- AAT GAA ACT AGT ACA CAA ACA TAT GAT TCA AA - #A AGA AAC AAT GGC CAT
1344
Asn Glu Thr Ser Thr Gln Thr Tyr Asp Ser Ly - #s Arg Asn Asn Gly His
# 445
- GTA AGT GCA CAG GAT TCT ATT GAC CAA TTA CC - #G CCA GAA ACA ACA GAT
1392
Val Ser Ala Gln Asp Ser Ile Asp Gln Leu Pr - #o Pro Glu Thr Thr Asp
# 460
- GAA CCA CTT GAA AAA GCA TAT AGT CAT CAG CT - #T AAT TAC GCG GAA TGT
1440
Glu Pro Leu Glu Lys Ala Tyr Ser His Gln Le - #u Asn Tyr Ala Glu Cys
465 4 - #70 4 - #75 4 -
#80
- TTC TTA ATG CAG GAC CGT CGT GGA ACA ATT CC - #A TTT TTT ACT TGG ACA
1488
Phe Leu Met Gln Asp Arg Arg Gly Thr Ile Pr - #o Phe Phe Thr Trp Thr
# 495
- CAT AGA AGT GTA GAC TTT TTT AAT ACA ATT GA - #T GCT GAA AAG ATT ACT
1536
His Arg Ser Val Asp Phe Phe Asn Thr Ile As - #p Ala Glu Lys Ile Thr
# 510
- CAA CTT CCA GTA GTG AAA GCA TAT GCC TTG TC - #T TCA GGT GCT TCC ATT
1584
Gln Leu Pro Val Val Lys Ala Tyr Ala Leu Se - #r Ser Gly Ala Ser Ile
# 525
- ATT GAA GGT CCA GGA TTC ACA GGA GGA AAT TT - #A CTA TTC CTA AAA GAA
1632
Ile Glu Gly Pro Gly Phe Thr Gly Gly Asn Le - #u Leu Phe Leu Lys Glu
# 540
- TCT AGT AAT TCA ATT GCT AAA TTT AAA GTT AC - #A TTA AAT TCA GCA GCC
1680
Ser Ser Asn Ser Ile Ala Lys Phe Lys Val Th - #r Leu Asn Ser Ala Ala
545 5 - #50 5 - #55 5 -
#60
- TTG TTA CAA CGA TAT CGT GTA AGA ATA CGC TA - #T GCT TCT ACC ACT AAC
1728
Leu Leu Gln Arg Tyr Arg Val Arg Ile Arg Ty - #r Ala Ser Thr Thr Asn
# 575
- TTA CGA CTT TTT GTG CAA AAT TCA AAC AAT GA - #T TTT CTT GTC ATC TAC
1776
Leu Arg Leu Phe Val Gln Asn Ser Asn Asn As - #p Phe Leu Val Ile Tyr
# 590
- ATT AAT AAA ACT ATG AAT AAA GAT GAT GAT TT - #A ACA TAT CAA ACA TTT
1824
Ile Asn Lys Thr Met Asn Lys Asp Asp Asp Le - #u Thr Tyr Gln Thr Phe
# 605
- GAT CTC GCA ACT ACT AAT TCT AAT ATG GGG TT - #C TCG GGT GAT AAG AAT
1872
Asp Leu Ala Thr Thr Asn Ser Asn Met Gly Ph - #e Ser Gly Asp Lys Asn
# 620
- GAA CTT ATA ATA GGA GCA GAA TCT TTC GTT TC - #T AAT GAA AAA ATC TAT
1920
Glu Leu Ile Ile Gly Ala Glu Ser Phe Val Se - #r Asn Glu Lys Ile Tyr
625 6 - #30 6 - #35 6 -
#40
# 1956AAG ATA GAA TTT ATC CCA GTA CAA TT - #G TAA
Ile Asp Lys Ile Glu Phe Ile Pro Val Gln Le - #u
# 650
- (2) INFORMATION FOR SEQ ID NO:58:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 651 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:58:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Glu Asp Pro Trp Ly - #s Ala Phe Met Ala Gln
# 110
- Val Glu Val Leu Ile Asp Lys Lys Ile Glu Gl - #u Tyr Ala Lys Ser Lys
# 125
- Ala Leu Ala Glu Leu Gln Gly Leu Gln Asn As - #n Phe Glu Asp Tyr Val
# 140
- Asn Ala Leu Asn Ser Trp Lys Lys Phe His Hi - #s Ser Arg Arg Ser Lys
145 1 - #50 1 - #55 1 -
#60
- Arg Ser Gln Asp Arg Ile Arg Glu Leu Phe Se - #r Gln Ala Glu Ser His
# 175
- Phe Arg Asn Ser Met Pro Ser Phe Ala Val Se - #r Lys Phe Glu Val Leu
# 190
- Phe Leu Pro Thr Tyr Ala Gln Ala Ala Asn Th - #r His Leu Leu Leu Leu
# 205
- Lys Asp Ala Gln Val Phe Gly Glu Glu Trp Gl - #y Tyr Ser Ser Glu Asp
# 220
- Val Ala Glu Phe Tyr His Arg Gln Leu Lys Le - #u Thr Gln Gln Tyr Thr
225 2 - #30 2 - #35 2 -
#40
- Asp His Cys Val Asn Trp Tyr Asn Val Gly Le - #u Asn Gly Leu Arg Gly
# 255
- Ser Thr Tyr Asp Ala Trp Val Lys Phe Asn Ar - #g Phe Arg Arg Glu Met
# 270
- Thr Leu Thr Val Leu Asp Leu Ile Val Leu Ph - #e Pro Phe Tyr Asp Ile
# 285
- Arg Leu Tyr Ser Lys Gly Val Lys Thr Glu Le - #u Thr Arg Asp Ile Phe
# 300
- Thr Asp Pro Ile Phe Ser Leu Asn Thr Leu Gl - #n Glu Tyr Gly Pro Thr
305 3 - #10 3 - #15 3 -
#20
- Phe Leu Ser Ile Glu Asn Ser Ile Arg Lys Pr - #o His Leu Phe Asp Tyr
# 335
- Leu Gln Gly Ile Glu Phe His Thr Arg Leu Gl - #n Pro Gly Tyr Phe Gly
# 350
- Lys Asp Ser Phe Asn Tyr Trp Ser Gly Asn Ty - #r Val Glu Thr Arg Pro
# 365
- Ser Ile Gly Ser Ser Lys Thr Ile Thr Ser Pr - #o Phe Tyr Gly Asp Lys
# 380
- Ser Thr Glu Pro Val Gln Lys Leu Ser Phe As - #p Gly Gln Lys Val Tyr
385 3 - #90 3 - #95 4 -
#00
- Arg Thr Ile Ala Asn Thr Asp Val Ala Ala Tr - #p Pro Asn Gly Lys Val
# 415
- Tyr Leu Gly Val Thr Lys Val Asp Phe Ser Gl - #n Tyr Asp Asp Gln Lys
# 430
- Asn Glu Thr Ser Thr Gln Thr Tyr Asp Ser Ly - #s Arg Asn Asn Gly His
# 445
- Val Ser Ala Gln Asp Ser Ile Asp Gln Leu Pr - #o Pro Glu Thr Thr Asp
# 460
- Glu Pro Leu Glu Lys Ala Tyr Ser His Gln Le - #u Asn Tyr Ala Glu Cys
465 4 - #70 4 - #75 4 -
#80
- Phe Leu Met Gln Asp Arg Arg Gly Thr Ile Pr - #o Phe Phe Thr Trp Thr
# 495
- His Arg Ser Val Asp Phe Phe Asn Thr Ile As - #p Ala Glu Lys Ile Thr
# 510
- Gln Leu Pro Val Val Lys Ala Tyr Ala Leu Se - #r Ser Gly Ala Ser Ile
# 525
- Ile Glu Gly Pro Gly Phe Thr Gly Gly Asn Le - #u Leu Phe Leu Lys Glu
# 540
- Ser Ser Asn Ser Ile Ala Lys Phe Lys Val Th - #r Leu Asn Ser Ala Ala
545 5 - #50 5 - #55 5 -
#60
- Leu Leu Gln Arg Tyr Arg Val Arg Ile Arg Ty - #r Ala Ser Thr Thr Asn
# 575
- Leu Arg Leu Phe Val Gln Asn Ser Asn Asn As - #p Phe Leu Val Ile Tyr
# 590
- Ile Asn Lys Thr Met Asn Lys Asp Asp Asp Le - #u Thr Tyr Gln Thr Phe
# 605
- Asp Leu Ala Thr Thr Asn Ser Asn Met Gly Ph - #e Ser Gly Asp Lys Asn
# 620
- Glu Leu Ile Ile Gly Ala Glu Ser Phe Val Se - #r Asn Glu Lys Ile Tyr
625 6 - #30 6 - #35 6 -
#40
- Ile Asp Lys Ile Glu Phe Ile Pro Val Gln Le - #u
# 650
- (2) INFORMATION FOR SEQ ID NO:59:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:59:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GGT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT ACC CTT AAT ACA CT - #A CAG AAG TAC GGA CCA
960
Phe Thr Asp Pro Ile Phe Thr Leu Asn Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:60:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:60:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Thr Leu Asn Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:61:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:61:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GGT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- GTT CGG TTA TAC CCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TCT ACG GAT CCA ATT TTT GCC GTT AAT ACT CT - #G TGG GAA TAC GGA CCA
960
Ser Thr Asp Pro Ile Phe Ala Val Asn Thr Le - #u Trp Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CGA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Arg Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GCA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Ala Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:62:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:62:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Ser Thr Asp Pro Ile Phe Ala Val Asn Thr Le - #u Trp Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Arg Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Ala Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:63:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:63:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- GTT CGG TTA TAC CCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CGA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Arg Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:64:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:64:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Val Arg Leu Tyr Pro Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Arg Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:65:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:65:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GGT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TTA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Leu Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:66:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:66:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Leu Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:67:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:67:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CGA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Arg Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:68:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:68:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Arg Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:69:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1482 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1479
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:69:
- AGT AAA AGA AGC CAA GAT CGA ATA AGG GAA CT - #T TTT TCT CAA GCA GAA
48
Ser Lys Arg Ser Gln Asp Arg Ile Arg Glu Le - #u Phe Ser Gln Ala Glu
# 15
- AGT CAT TTT CGT AAT TCC ATG CCG TCA TTT GC - #A GTT TCC AAA TTC GAA
96
Ser His Phe Arg Asn Ser Met Pro Ser Phe Al - #a Val Ser Lys Phe Glu
# 30
- GTG CTG TTT CTA CCA ACA TAT GCA CAA GCT GC - #A AAT ACA CAT TTA TTG
144
Val Leu Phe Leu Pro Thr Tyr Ala Gln Ala Al - #a Asn Thr His Leu Leu
# 45
- CTA TTA AAA GAT GCT CAA GTT TTT GGA GAA GA - #A TGG GGA TAT TCT TCA
192
Leu Leu Lys Asp Ala Gln Val Phe Gly Glu Gl - #u Trp Gly Tyr Ser Ser
# 60
- GAA GAT GTT GCT GAA TTT TAT CAT AGA CAA TT - #A AAA CTT ACA CAA CAA
240
Glu Asp Val Ala Glu Phe Tyr His Arg Gln Le - #u Lys Leu Thr Gln Gln
# 80
- TAC ACT GAC CAT TGT GTT AAT TGG TAT AAT GT - #T GGA TTA AAT GGT TTA
288
Tyr Thr Asp His Cys Val Asn Trp Tyr Asn Va - #l Gly Leu Asn Gly Leu
# 95
- AGA GGT TCA ACT TAT GAT GCA TGG GTC AAA TT - #T AAC CGT TTT CGC AGA
336
Arg Gly Ser Thr Tyr Asp Ala Trp Val Lys Ph - #e Asn Arg Phe Arg Arg
# 110
- GAA ATG ACT TTA ACT GTA TTA GAT CTA ATT GT - #A CTT TTC CCA TTT TAT
384
Glu Met Thr Leu Thr Val Leu Asp Leu Ile Va - #l Leu Phe Pro Phe Tyr
# 125
- GAT ATT CGG TTA TAC TCA AAA GGG GTT AAA AC - #A GAA CTA ACA AGA GAC
432
Asp Ile Arg Leu Tyr Ser Lys Gly Val Lys Th - #r Glu Leu Thr Arg Asp
# 140
- ATT TTT ACG GAT CCA ATT TTT TCA CTT AAT AC - #T CTT CAG GAG TAT GGA
480
Ile Phe Thr Asp Pro Ile Phe Ser Leu Asn Th - #r Leu Gln Glu Tyr Gly
145 1 - #50 1 - #55 1 -
#60
- CCA ACT TTT TTG AGT ATA GAA AAC TCT ATT CG - #A AAA CCT CAT TTA TTT
528
Pro Thr Phe Leu Ser Ile Glu Asn Ser Ile Ar - #g Lys Pro His Leu Phe
# 175
- GAT TAT TTA CAG GGG ATT GAA TTT CAT ACG CG - #T CTT CAA CCT GGT TAC
576
Asp Tyr Leu Gln Gly Ile Glu Phe His Thr Ar - #g Leu Gln Pro Gly Tyr
# 190
- TTT GGG AAA GAT TCT TTC AAT TAT TGG TCT GG - #T AAT TAT GTA GAA ACT
624
Phe Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gl - #y Asn Tyr Val Glu Thr
# 205
- AGA CCT AGT ATA GGA TCT AGT AAG ACA ATT AC - #T TCC CCA TTT TAT GGA
672
Arg Pro Ser Ile Gly Ser Ser Lys Thr Ile Th - #r Ser Pro Phe Tyr Gly
# 220
- GAT AAA TCT ACT GAA CCT GTA CAA AAG CTA AG - #C TTT GAT GGA CAA AAA
720
Asp Lys Ser Thr Glu Pro Val Gln Lys Leu Se - #r Phe Asp Gly Gln Lys
225 2 - #30 2 - #35 2 -
#40
- GTT TAT CGA ACT ATA GCT AAT ACA GAC GTA GC - #G GCT TGG CCG AAT GGT
768
Val Tyr Arg Thr Ile Ala Asn Thr Asp Val Al - #a Ala Trp Pro Asn Gly
# 255
- AAG GTA TAT TTA GGT GTT ACG AAA GTT GAT TT - #T AGT CAA TAT GAT GAT
816
Lys Val Tyr Leu Gly Val Thr Lys Val Asp Ph - #e Ser Gln Tyr Asp Asp
# 270
- CAA AAA AAT GAA ACT AGT ACA CAA ACA TAT GA - #T TCA AAA AGA AAC AAT
864
Gln Lys Asn Glu Thr Ser Thr Gln Thr Tyr As - #p Ser Lys Arg Asn Asn
# 285
- GGC CAT GTA AGT GCA CAG GAT TCT ATT GAC CA - #A TTA CCG CCA GAA ACA
912
Gly His Val Ser Ala Gln Asp Ser Ile Asp Gl - #n Leu Pro Pro Glu Thr
# 300
- ACA GAT GAA CCA CTT GAA AAA GCA TAT AGT CA - #T CAG CTT AAT TAC GCG
960
Thr Asp Glu Pro Leu Glu Lys Ala Tyr Ser Hi - #s Gln Leu Asn Tyr Ala
305 3 - #10 3 - #15 3 -
#20
- GAA TGT TTC TTA ATG CAG GAC CGT CGT GGA AC - #A ATT CCA TTT TTT ACT
1008
Glu Cys Phe Leu Met Gln Asp Arg Arg Gly Th - #r Ile Pro Phe Phe Thr
# 335
- TGG ACA CAT AGA AGT GTA GAC TTT TTT AAT AC - #A ATT GAT GCT GAA AAG
1056
Trp Thr His Arg Ser Val Asp Phe Phe Asn Th - #r Ile Asp Ala Glu Lys
# 350
- ATT ACT CAA CTT CCA GTA GTG AAA GCA TAT GC - #C TTG TCT TCA GGT GCT
1104
Ile Thr Gln Leu Pro Val Val Lys Ala Tyr Al - #a Leu Ser Ser Gly Ala
# 365
- TCC ATT ATT GAA GGT CCA GGA TTC ACA GGA GG - #A AAT TTA CTA TTC CTA
1152
Ser Ile Ile Glu Gly Pro Gly Phe Thr Gly Gl - #y Asn Leu Leu Phe Leu
# 380
- AAA GAA TCT AGT AAT TCA ATT GCT AAA TTT AA - #A GTT ACA TTA AAT TCA
1200
Lys Glu Ser Ser Asn Ser Ile Ala Lys Phe Ly - #s Val Thr Leu Asn Ser
385 3 - #90 3 - #95 4 -
#00
- GCA GCC TTG TTA CAA CGA TAT CGT GTA AGA AT - #A CGC TAT GCT TCT ACC
1248
Ala Ala Leu Leu Gln Arg Tyr Arg Val Arg Il - #e Arg Tyr Ala Ser Thr
# 415
- ACT AAC TTA CGA CTT TTT GTG CAA AAT TCA AA - #C AAT GAT TTT CTT GTC
1296
Thr Asn Leu Arg Leu Phe Val Gln Asn Ser As - #n Asn Asp Phe Leu Val
# 430
- ATC TAC ATT AAT AAA ACT ATG AAT AAA GAT GA - #T GAT TTA ACA TAT CAA
1344
Ile Tyr Ile Asn Lys Thr Met Asn Lys Asp As - #p Asp Leu Thr Tyr Gln
# 445
- ACA TTT GAT CTC GCA ACT ACT AAT TCT AAT AT - #G GGG TTC TCG GGT GAT
1392
Thr Phe Asp Leu Ala Thr Thr Asn Ser Asn Me - #t Gly Phe Ser Gly Asp
# 460
- AAG AAT GAA CTT ATA ATA GGA GCA GAA TCT TT - #C GTT TCT AAT GAA AAA
1440
Lys Asn Glu Leu Ile Ile Gly Ala Glu Ser Ph - #e Val Ser Asn Glu Lys
465 4 - #70 4 - #75 4 -
#80
- ATC TAT ATA GAT AAG ATA GAA TTT ATC CCA GT - #A CAA TTG TAA
#1482
Ile Tyr Ile Asp Lys Ile Glu Phe Ile Pro Va - #l Gln Leu
# 490
- (2) INFORMATION FOR SEQ ID NO:70:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 493 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:70:
- Ser Lys Arg Ser Gln Asp Arg Ile Arg Glu Le - #u Phe Ser Gln Ala Glu
# 15
- Ser His Phe Arg Asn Ser Met Pro Ser Phe Al - #a Val Ser Lys Phe Glu
# 30
- Val Leu Phe Leu Pro Thr Tyr Ala Gln Ala Al - #a Asn Thr His Leu Leu
# 45
- Leu Leu Lys Asp Ala Gln Val Phe Gly Glu Gl - #u Trp Gly Tyr Ser Ser
# 60
- Glu Asp Val Ala Glu Phe Tyr His Arg Gln Le - #u Lys Leu Thr Gln Gln
# 80
- Tyr Thr Asp His Cys Val Asn Trp Tyr Asn Va - #l Gly Leu Asn Gly Leu
# 95
- Arg Gly Ser Thr Tyr Asp Ala Trp Val Lys Ph - #e Asn Arg Phe Arg Arg
# 110
- Glu Met Thr Leu Thr Val Leu Asp Leu Ile Va - #l Leu Phe Pro Phe Tyr
# 125
- Asp Ile Arg Leu Tyr Ser Lys Gly Val Lys Th - #r Glu Leu Thr Arg Asp
# 140
- Ile Phe Thr Asp Pro Ile Phe Ser Leu Asn Th - #r Leu Gln Glu Tyr Gly
145 1 - #50 1 - #55 1 -
#60
- Pro Thr Phe Leu Ser Ile Glu Asn Ser Ile Ar - #g Lys Pro His Leu Phe
# 175
- Asp Tyr Leu Gln Gly Ile Glu Phe His Thr Ar - #g Leu Gln Pro Gly Tyr
# 190
- Phe Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gl - #y Asn Tyr Val Glu Thr
# 205
- Arg Pro Ser Ile Gly Ser Ser Lys Thr Ile Th - #r Ser Pro Phe Tyr Gly
# 220
- Asp Lys Ser Thr Glu Pro Val Gln Lys Leu Se - #r Phe Asp Gly Gln Lys
225 2 - #30 2 - #35 2 -
#40
- Val Tyr Arg Thr Ile Ala Asn Thr Asp Val Al - #a Ala Trp Pro Asn Gly
# 255
- Lys Val Tyr Leu Gly Val Thr Lys Val Asp Ph - #e Ser Gln Tyr Asp Asp
# 270
- Gln Lys Asn Glu Thr Ser Thr Gln Thr Tyr As - #p Ser Lys Arg Asn Asn
# 285
- Gly His Val Ser Ala Gln Asp Ser Ile Asp Gl - #n Leu Pro Pro Glu Thr
# 300
- Thr Asp Glu Pro Leu Glu Lys Ala Tyr Ser Hi - #s Gln Leu Asn Tyr Ala
305 3 - #10 3 - #15 3 -
#20
- Glu Cys Phe Leu Met Gln Asp Arg Arg Gly Th - #r Ile Pro Phe Phe Thr
# 335
- Trp Thr His Arg Ser Val Asp Phe Phe Asn Th - #r Ile Asp Ala Glu Lys
# 350
- Ile Thr Gln Leu Pro Val Val Lys Ala Tyr Al - #a Leu Ser Ser Gly Ala
# 365
- Ser Ile Ile Glu Gly Pro Gly Phe Thr Gly Gl - #y Asn Leu Leu Phe Leu
# 380
- Lys Glu Ser Ser Asn Ser Ile Ala Lys Phe Ly - #s Val Thr Leu Asn Ser
385 3 - #90 3 - #95 4 -
#00
- Ala Ala Leu Leu Gln Arg Tyr Arg Val Arg Il - #e Arg Tyr Ala Ser Thr
# 415
- Thr Asn Leu Arg Leu Phe Val Gln Asn Ser As - #n Asn Asp Phe Leu Val
# 430
- Ile Tyr Ile Asn Lys Thr Met Asn Lys Asp As - #p Asp Leu Thr Tyr Gln
# 445
- Thr Phe Asp Leu Ala Thr Thr Asn Ser Asn Me - #t Gly Phe Ser Gly Asp
# 460
- Lys Asn Glu Leu Ile Ile Gly Ala Glu Ser Ph - #e Val Ser Asn Glu Lys
465 4 - #70 4 - #75 4 -
#80
- Ile Tyr Ile Asp Lys Ile Glu Phe Ile Pro Va - #l Gln Leu
# 490
- (2) INFORMATION FOR SEQ ID NO:71:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 23 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:71:
# 23AAAG ATG
- (2) INFORMATION FOR SEQ ID NO:72:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 20 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:72:
# 20 AATC
- (2) INFORMATION FOR SEQ ID NO:73:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 39 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 21..23
#/note= "N = A, T, G, C"RMATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:73:
# 39 ATTC NNNCATAGAC AATTAAAAC
- (2) INFORMATION FOR SEQ ID NO:74:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 34 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 19..21
#/note= "N = A, T, G, C"RMATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:74:
# 34 ATNN NAGACAATTA AAAC
- (2) INFORMATION FOR SEQ ID NO:75:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 33 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 17
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 18
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 19
#/note= "N = A, T, G or C"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:75:
# 33 NNNT TATACTCAAA AGG
- (2) INFORMATION FOR SEQ ID NO:76:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 64 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 24
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 27, 28, 30, 34, 36, 39, 43)of(25,
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 33, 35, 37, 42, 44)ON: one-of(31,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 40
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 29, 32, 38, 41)CATION: one-of(26,
#/note= "N = A, T, G or C"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:76:
- AGCTATGCTG GTCTCGGAAG AAANNNNNNN NNNNNNNNNN NNNNAAAAGA AG - #CCAAGATC
60
# 64
- (2) INFORMATION FOR SEQ ID NO:77:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 40 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:77:
# 40 CTTC CAGGAATTTA ACGCATTAAC
- (2) INFORMATION FOR SEQ ID NO:78:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 65 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 27, 29, 30, 37, 42)ON: one-of(22,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 26, 28, 31, 38, 40, 43, 44)of(23,
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
#39) (B) LOCATION: one-of(24,
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 32, 33, 41, 46, 47, 48)one-of(25,
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 34
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 45
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 35..36
#/note= "N = A, G, C or T"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:78:
- AGCTATGCTG GTCTCCCATT TNNNNNNNNN NNNNNNNNNN NNNNNNNNGT TA - #AAACAGAA
60
# 65
- (2) INFORMATION FOR SEQ ID NO:79:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 36 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:79:
# 36 AATG GGAAAAGTAC AATTAG
- (2) INFORMATION FOR SEQ ID NO:80:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 63 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 27, 31, 36, 44)CATION: one-of(23,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 25, 26, 33, 35, 38)ON: one-of(24,
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 34, 37) (B) LOCATION: one-of(28,
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 30, 32, 39, 42, 45)ON: one-of(29,
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
#43) (B) LOCATION: one-of(40,
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 41
#/note= "N = A, C, T or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 46
#/note= "N = A, T, G or C"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:80:
- CATTTTTACG GATCCAATTT TTNNNNNNNN NNNNNNNNNN NNNNNNGGAC CA - #ACTTTTTT
60
# 63
- (2) INFORMATION FOR SEQ ID NO:81:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 62 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 31, 32, 33, 42)CATION: one-of(28,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 38, 39, 41)) LOCATION: one-of(29,
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 30
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 35, 40) (B) LOCATION: one-of(34,
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 36
#/note= "N = A, T, G, C"RMATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 37
#/note= "N = A, T, G or C"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:81:
- GAATTTCATA CGCGTCTTCA ACCTGGTNNN NNNNNNNNNN NNTCTTTCAA TT - #ATTGGTCT
60
# 62
- (2) INFORMATION FOR SEQ ID NO:82:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 73 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 49, 52) (B) LOCATION: one-of(41,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 42..43
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 44..45
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 46
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 48, 53, 54)) LOCATION: one-of(47,
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 51, 55) (B) LOCATION: one-of(50,
#/note= "N = A, T, C or G"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:82:
- AAAAGTTTAT CGAACTATAG CTAATACAGA CGTAGCGGCT NNNNNNNNNN NN - #NNNGTATA
60
# 73
- (2) INFORMATION FOR SEQ ID NO:83:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 20 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:83:
# 20 GGGC
- (2) INFORMATION FOR SEQ ID NO:84:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 17 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:84:
# 17 G
- (2) INFORMATION FOR SEQ ID NO:85:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 32 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:85:
# 32 CAAG GTCGAATAAG GG
- (2) INFORMATION FOR SEQ ID NO:86:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 43 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:86:
# 43 ATCC ACACAGCCAA GGTCGAATAA GGG
- (2) INFORMATION FOR SEQ ID NO:87:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 35 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:87:
# 35 CGGT TATACCCAAA AGGGG
- (2) INFORMATION FOR SEQ ID NO:88:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 25 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:88:
# 25 ATGG AAGGC
- (2) INFORMATION FOR SEQ ID NO:89:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 22 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:89:
# 22AGT GC
- (2) INFORMATION FOR SEQ ID NO:90:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 17 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:90:
# 17 A
- (2) INFORMATION FOR SEQ ID NO:91:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 17 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:91:
# 17 A
- (2) INFORMATION FOR SEQ ID NO:92:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 60 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 26, 29) (B) LOCATION: one-of(22,
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 33, 36) (B) LOCATION: one-of(23,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 27, 28, 32, 35, 37, 38)one-of(24,
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 30, 31, 34)) LOCATION: one-of(25,
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 39
#/note= "N = A, T, G or C"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:92:
- AGCTATGCTG GTCTCTTCTT ANNNNNNNNN NNNNNNNNNA CAATTCCATT TT - #TTACTTGG
60
- (2) INFORMATION FOR SEQ ID NO:93:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 40 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:93:
# 40 AAGA AACAAACCGC GTAATTAAGC
- (2) INFORMATION FOR SEQ ID NO:94:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 20 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:94:
# 20 ATCC
- (2) INFORMATION FOR SEQ ID NO:95:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 55 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 22, 23, 31)) LOCATION: one-of(19,
#/note= "N = A, T, C or G"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 26, 27, 29, 30, 35)ON: one-of(20,
#/note= "N = T, G, C or A"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
# 32, 34) (B) LOCATION: one-of(21,
#/note= "N = A, G, C or T"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
#33) (B) LOCATION: one-of(24,
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 25
#/note= "N = A, G, T or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 28
#/note= "N = A, T, G or C"ATION:
- (ix) FEATURE:
(A) NAME/KEY: modified.sub.-- - #base
(B) LOCATION: 36
#/note= "N = A, G, C or T"ATION:
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:95:
- GTACAAAAGC TAAGCTTTNN NNNNNNNNNN NNNNNNCGAA CTATAGCTAA TA - #CAG
55
- (2) INFORMATION FOR SEQ ID NO:96:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 7 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:96:
- Ser Lys Arg Ser Gln Asp Arg
1 5
- (2) INFORMATION FOR SEQ ID NO:97:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (ix) FEATURE:
(A) NAME/KEY: CDS
(B) LOCATION: 1..1956
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:97:
- ATG AAT CCA AAC AAT CGA AGT GAA CAT GAT AC - #G ATA AAG GTT ACA CCT
48
Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- AAC AGT GAA TTG CAA ACT AAC CAT AAT CAA TA - #T CCT TTA GCT GAC AAT
96
Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- CCA AAT TCA ACA CTA GAA GAA TTA AAT TAT AA - #A GAA TTT TTA AGA ATG
144
Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- ACT GAA GAC AGT TCT ACG GAA GTG CTA GAC AA - #C TCT ACA GTA AAA GAT
192
Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- GCA GTT GGG ACA GGA ATT TCT GTT GTA GGG CA - #G ATT TTA GGT GTT GTA
240
Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- GGA GTT CCA TTT GCT GGG GCA CTC ACT TCA TT - #T TAT CAA TCA TTT CTT
288
Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- AAC ACT ATA TGG CCA AGT GAT GCT GAC CCA TG - #G AAG GCT TTT ATG GCA
336
Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- CAA GTT GAA GTA CTG ATA GAT AAG AAA ATA GA - #G GAG TAT GCT AAA AGT
384
Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- AAA GCT CTT GCA GAG TTA CAG GGT CTT CAA AA - #T AAT TTC GAA GAT TAT
432
Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- GTT AAT GCG TTA AAT TCC TGG AAG AAA ACA CC - #T TTA AGT TTG CGA AGT
480
Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- AAA AGA AGC CAA GAT CGA ATA AGG GAA CTT TT - #T TCT CAA GCA GAA AGT
528
Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- CAT TTT CGT AAT TCC ATG CCG TCA TTT GCA GT - #T TCC AAA TTC GAA GTG
576
His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- CTG TTT CTA CCA ACA TAT GCA CAA GCT GCA AA - #T ACA CAT TTA TTG CTA
624
Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- TTA AAA GAT GCT CAA GTT TTT GGA GAA GAA TG - #G GGA TAT TCT TCA GAA
672
Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- GAT GTT GCT GAA TTT TAT CAT AGA CAA TTA AA - #A CTT ACA CAA CAA TAC
720
Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- ACT GAC CAT TGT GTT AAT TGG TAT AAT GTT GG - #A TTA AAT GGT TTA AGA
768
Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- GGT TCA ACT TAT GAT GCA TGG GTC AAA TTT AA - #C CGT TTT CGC AGA GAA
816
Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- ATG ACT TTA ACT GTA TTA GAT CTA ATT GTA CT - #T TTC CCA TTT TAT GAT
864
Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- ATT CGG TTA TAC TCA AAA GGG GTT AAA ACA GA - #A CTA ACA AGA GAC ATT
912
Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- TTT ACG GAT CCA ATT TTT TCA CTT AAT ACT CT - #T CAG GAG TAT GGA CCA
960
Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- ACT TTT TTG AGT ATA GAA AAC TCT ATT CGA AA - #A CCT CAT TTA TTT GAT
1008
Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- TAT TTA CAG GGG ATT GAA TTT CAT ACG CGT CT - #T CAA CCT GGT TAC TTT
1056
Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- GGG AAA GAT TCT TTC AAT TAT TGG TCT GGT AA - #T TAT GTA GAA ACT AGA
1104
Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- CCT AGT ATA GGA TCT AGT AAG ACA ATT ACT TC - #C CCA TTT TAT GGA GAT
1152
Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- AAA TCT ACT GAA CCT GTA CAA AAG CTA AGC TT - #T GAT GGA CAA AAA GTT
1200
Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- TAT CGA ACT ATA GCT AAT ACA GAC GTA GCG GC - #T TGG CCG AAT GGT AAG
1248
Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- GTA TAT TTA GGT GTT ACG AAA GTT GAT TTT AG - #T CAA TAT GAT GAT CAA
1296
Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- AAA AAT GAA ACT AGT ACA CAA ACA TAT GAT TC - #A AAA AGA AAC AAT GGC
1344
Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- CAT GTA AGT GCA CAG GAT TCT ATT GAC CAA TT - #A CCG CCA GAA ACA ACA
1392
His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- GAT GAA CCA CTT GAA AAA GCA TAT AGT CAT CA - #G CTT AAT TAC GCG GAA
1440
Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- TGT TTC TTA ATG CAG GAC CGT CGT GGA ACA AT - #T CCA TTT TTT ACT TGG
1488
Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- ACA CAT AGA AGT GTA GAC TTT TTT AAT ACA AT - #T GAT GCT GAA AAG ATT
1536
Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- ACT CAA CTT CCA GTA GTG AAA GCA TAT GCC TT - #G TCT TCA GGT GCT TCC
1584
Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- ATT ATT GAA GGT CCA GGA TTC ACA GGA GGA AA - #T TTA CTA TTC CTA AAA
1632
Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- GAA TCT AGT AAT TCA ATT GCT AAA TTT AAA GT - #T ACA TTA AAT TCA GCA
1680
Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- GCC TTG TTA CAA CGA TAT CGT GTA AGA ATA CG - #C TAT GCT TCT ACC ACT
1728
Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- AAC TTA CGA CTT TTT GTG CAA AAT TCA AAC AA - #T GAT TTT CTT GTC ATC
1776
Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- TAC ATT AAT AAA ACT ATG AAT AAA GAT GAT GA - #T TTA ACA TAT CAA ACA
1824
Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- TTT GAT CTC GCA ACT ACT AAT TCT AAT ATG GG - #G TTC TCG GGT GAT AAG
1872
Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- AAT GAA CTT ATA ATA GGA GCA GAA TCT TTC GT - #T TCT AAT GAA AAA ATC
1920
Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
# 1959A GAT AAG ATA GAA TTT ATC CCA GTA CA - #A TTG TAA
Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:98:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(D) TOPOLOGY: linear
- (ii) MOLECULE TYPE: protein
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:98:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
# 80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:99:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 2000 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:99:
- CCATCCATGG CAAACCCTAA CAATCGTTCC GAACACGACA CCATCAAGGT TA - #CTCCAAAC
60
- TCTGAGTTGC AAACTAATCA CAACCAGTAC CCATTGGCTG ACAATCCTAA CA - #GTACTCTT
120
- GAGGAACTTA ACTACAAGGA GTTTCTCCGG ATGACCGAAG ATAGCTCCAC TG - #AGGTTCTC
180
- GATAACTCTA CAGTGAAGGA CGCTGTTGGA ACTGGCATTA GCGTTGTGGG AC - #AGATTCTT
240
- GGAGTGGTTG GTGTTCCATT CGCTGGAGCT TTGACCAGCT TCTACCAGTC CT - #TTCTCAAC
300
- ACCATCTGGC CTTCAGATGC TGATCCCTGG AAGGCTTTCA TGGCCCAAGT GG - #AAGTCTTG
360
- ATCGATAAGA AGATCGAAGA GTATGCCAAG TCTAAAGCCT TGGCTGAGTT GC - #AAGGTTTG
420
- CAGAACAACT TCGAGGATTA CGTCAACGCA CTCAACAGCT GGAAGAAAAC TC - #CCTTGAGT
480
- CTCAGGTCTA AGCGTTCCCA GGACCGTATT CGTGAACTTT TCAGCCAAGC CG - #AATCCCAC
540
- TTCAGAAACT CCATGCCTAG CTTTGCCGTT TCTAAGTTCG AGGTGCTCTT CT - #TGCCAACA
600
- TACGCACAAG CTGCCAACAC TCATCTCTTG CTTCTCAAAG ACGCTCAGGT GT - #TTGGTGAG
660
- GAATGGGGTT ACTCCAGTGA AGATGTTGCC GAGTTCTACC GTAGGCAGCT CA - #AGTTGACT
720
- CAACAGTACA CAGACCACTG CGTCAACTGG TACAACGTTG GGCTCAATGG TC - #TTAGAGGA
780
- TCTACCTACG ACGCATGGGT GAAGTTCAAC AGGTTTCGTA GAGAGATGAC CT - #TGACTGTG
840
- CTCGATCTTA TCGTTCTCTT TCCATTCTAC GACATTCGTC TTTACTCCAA AG - #GCGTTAAG
900
- ACAGAGCTGA CCAGAGACAT CTTCACCGAT CCCATCTTCC TACTTACGAC CC - #TGCAGAAA
960
- TACGGTCCAA CTTTTCTCTC CATTGAGAAC AGCATCAGGA AGCCTCACCT CT - #TCGACTAT
1020
- CTGCAAGGCA TTGAGTTTCA CACCAGGTTG CAACCTGGTT ACTTCGGTAA GG - #ATTCCTTC
1080
- AACTACTGGA GCGGAAACTA CGTTGAAACC AGACCATCCA TCGGATCTAG CA - #AGACCATC
1140
- ACTTCTCCAT TCTACGGTGA CAAGAGCACT GAGCCAGTGC AGAAGTTGAG CT - #TCGATGGG
1200
- CAGAAGGTGT ATAGAACCAT CGCCAATACC GATGTTGCAG CTTGGCCTAA TG - #GCAAGGTC
1260
- TACCTTGGAG TTACTAAAGT GGACTTCTCC CAATACGACG ATCAGAAGAA CG - #AGACATCT
1320
- ACTCAAACCT ACGATAGTAA GAGGAACAAT GGCCATGTTT CCGCACAAGA CT - #CCATTGAC
1380
- CAACTTCCAC CTGAAACCAC TGATGAACCA TTGGAGAAGG CTTACAGTCA CC - #AACTTAAC
1440
- TACGCCGAAT GCTTTCTCAT GCAAGACAGG CGTGGCACCA TTCCGTTCTT TA - #CATGGACT
1500
- CACAGGTCTG TCGACTTCTT TAACACTATC GACGCTGAGA AGATTACCCA AC - #TTCCCGTG
1560
- GTCAAGGCTT ATGCCTTGTC CAGCGGAGCT TCCATCATTG AAGGTCCAGG CT - #TCACCGGT
1620
- GGCAACTTGC TCTTCCTTAA GGAGTCCAGC AACTCCATCG CCAAGTTCAA AG - #TGACACTT
1680
- AACTCAGCAG CCTTGCTCCA ACGTTACAGG GTTCGTATCA GATACGCAAG CA - #CTACCAAT
1740
- CTTCGCCTCT TTGTCCAGAA CAGCAACAAT GATTTCCTTG TCATCTACAT CA - #ACAAGACT
1800
- ATGAACAAAG ACGATGACCT CACCTACCAA ACATTCGATC TTGCCACTAC CA - #ATAGTAAC
1860
- ATGGGATTCT CTGGTGACAA GAACGAGCTG ATCATAGGTG CTGAGAGCTT TG - #TCTCTAAT
1920
- GAGAAGATTT ACATAGACAA GATCGAGTTC ATTCCAGTTC AACTCTAATA GA - #TCCCCCGG
1980
# 200 - #0
- (2) INFORMATION FOR SEQ ID NO:100:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 653 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:100:
- Met Ala Asn Pro Asn Asn Arg Ser Glu His As - #p Thr Ile Lys Val Thr
# 15
- Pro Asn Ser Glu Leu Gln Thr Asn His Asn Gl - #n Tyr Pro Leu Ala Asp
# 30
- Asn Pro Asn Ser Thr Leu Glu Glu Leu Asn Ty - #r Lys Glu Phe Leu Arg
# 45
- Met Thr Glu Asp Ser Ser Thr Glu Val Leu As - #p Asn Ser Thr Val Lys
# 60
- Asp Ala Val Gly Thr Gly Ile Ser Val Val Gl - #y Gln Ile Leu Gly Val
#80
- Val Gly Val Pro Phe Ala Gly Ala Leu Thr Se - #r Phe Tyr Gln Ser Phe
# 95
- Leu Asn Thr Ile Trp Pro Ser Asp Ala Asp Pr - #o Trp Lys Ala Phe Met
# 110
- Ala Gln Val Glu Val Leu Ile Asp Lys Lys Il - #e Glu Glu Tyr Ala Lys
# 125
- Ser Lys Ala Leu Ala Glu Leu Gln Gly Leu Gl - #n Asn Asn Phe Glu Asp
# 140
- Tyr Val Asn Ala Leu Asn Ser Trp Lys Lys Th - #r Pro Leu Ser Leu Arg
145 1 - #50 1 - #55 1 -
#60
- Ser Lys Arg Ser Gln Asp Arg Ile Arg Glu Le - #u Phe Ser Gln Ala Glu
# 175
- Ser His Phe Arg Asn Ser Met Pro Ser Phe Al - #a Val Ser Lys Phe Glu
# 190
- Val Leu Phe Leu Pro Thr Tyr Ala Gln Ala Al - #a Asn Thr His Leu Leu
# 205
- Leu Leu Lys Asp Ala Gln Val Phe Gly Glu Gl - #u Trp Gly Tyr Ser Ser
# 220
- Glu Asp Val Ala Glu Phe Tyr Arg Arg Gln Le - #u Lys Leu Thr Gln Gln
225 2 - #30 2 - #35 2 -
#40
- Tyr Thr Asp His Cys Val Asn Trp Tyr Asn Va - #l Gly Leu Asn Gly Leu
# 255
- Arg Gly Ser Thr Tyr Asp Ala Trp Val Lys Ph - #e Asn Arg Phe Arg Arg
# 270
- Glu Met Thr Leu Thr Val Leu Asp Leu Ile Va - #l Leu Phe Pro Phe Tyr
# 285
- Asp Ile Arg Leu Tyr Ser Lys Gly Val Lys Th - #r Glu Leu Thr Arg Asp
# 300
- Ile Phe Thr Asp Pro Ile Phe Leu Leu Thr Th - #r Leu Gln Lys Tyr Gly
305 3 - #10 3 - #15 3 -
#20
- Pro Thr Phe Leu Ser Ile Glu Asn Ser Ile Ar - #g Lys Pro His Leu Phe
# 335
- Asp Tyr Leu Gln Gly Ile Glu Phe His Thr Ar - #g Leu Gln Pro Gly Tyr
# 350
- Phe Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gl - #y Asn Tyr Val Glu Thr
# 365
- Arg Pro Ser Ile Gly Ser Ser Lys Thr Ile Th - #r Ser Pro Phe Tyr Gly
# 380
- Asp Lys Ser Thr Glu Pro Val Gln Lys Leu Se - #r Phe Asp Gly Gln Lys
385 3 - #90 3 - #95 4 -
#00
- Val Tyr Arg Thr Ile Ala Asn Thr Asp Val Al - #a Ala Trp Pro Asn Gly
# 415
- Lys Val Tyr Leu Gly Val Thr Lys Val Asp Ph - #e Ser Gln Tyr Asp Asp
# 430
- Gln Lys Asn Glu Thr Ser Thr Gln Thr Tyr As - #p Ser Lys Arg Asn Asn
# 445
- Gly His Val Ser Ala Gln Asp Ser Ile Asp Gl - #n Leu Pro Pro Glu Thr
# 460
- Thr Asp Glu Pro Leu Glu Lys Ala Tyr Ser Hi - #s Gln Leu Asn Tyr Ala
465 4 - #70 4 - #75 4 -
#80
- Glu Cys Phe Leu Met Gln Asp Arg Arg Gly Th - #r Ile Pro Phe Phe Thr
# 495
- Trp Thr His Arg Ser Val Asp Phe Phe Asn Th - #r Ile Asp Ala Glu Lys
# 510
- Ile Thr Gln Leu Pro Val Val Lys Ala Tyr Al - #a Leu Ser Ser Gly Ala
# 525
- Ser Ile Ile Glu Gly Pro Gly Phe Thr Gly Gl - #y Asn Leu Leu Phe Leu
# 540
- Lys Glu Ser Ser Asn Ser Ile Ala Lys Phe Ly - #s Val Thr Leu Asn Ser
545 5 - #50 5 - #55 5 -
#60
- Ala Ala Leu Leu Gln Arg Tyr Arg Val Arg Il - #e Arg Tyr Ala Ser Thr
# 575
- Thr Asn Leu Arg Leu Phe Val Gln Asn Ser As - #n Asn Asp Phe Leu Val
# 590
- Ile Tyr Ile Asn Lys Thr Met Asn Lys Asp As - #p Asp Leu Thr Tyr Gln
# 605
- Thr Phe Asp Leu Ala Thr Thr Asn Ser Asn Me - #t Gly Phe Ser Gly Asp
# 620
- Lys Asn Glu Leu Ile Ile Gly Ala Glu Ser Ph - #e Val Ser Asn Glu Lys
625 6 - #30 6 - #35 6 -
#40
- Ile Tyr Ile Asp Lys Ile Glu Phe Ile Pro Va - #l Gln Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:101:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 2050 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:101:
- TGGAGCTCCA CCGCGGTGGC GGCCGCTCTA GAACTAGTGG ATCTAGGCCT CC - #ATATGAAC
60
- CCTAACAATC GTTCCGAACA CGACACCATC AAGGTTACTC CAAACTCTGA GT - #TGCAAACT
120
- AATCACAACC AGTACCCATT GGCTGACAAT CCTAACAGTA CTCTTGAGGA AC - #TTAACTAC
180
- AAGGAGTTTC TCCGGATGAC CGAAGATAGC TCCACTGAGG TTCTCGATAA CT - #CTACAGTG
240
- AAGGACGCTG TTGGAACTGG CATTAGCGTT GTGGGACAGA TTCTTGGAGT GG - #TTGGTGTT
300
- CCATTCGCTG GAGCTTTGAC CAGCTTCTAC CAGTCCTTTC TCAACACCAT CT - #GGCCTTCA
360
- GATGCTGATC CCTGGAAGGC TTTCATGGCC CAAGTGGAAG TCTTGATCGA TA - #AGAAGATC
420
- GAAGAGTATG CCAAGTCTAA AGCCTTGGCT GAGTTGCAAG GTTTGCAGAA CA - #ACTTCGAG
480
- GATTACGTCA ACGCACTCAA CAGCTGGAAG AAAACTCCCT TGAGTCTCAG GT - #CTAAGCGT
540
- TCCCAGGACC GTATTCGTGA ACTTTTCAGC CAAGCCGAAT CCCACTTCAG AA - #ACTCCATG
600
- CCTAGCTTTG CCGTTTCTAA GTTCGAGGTG CTCTTCTTGC CAACATACGC AC - #AAGCTGCC
660
- AACACTCATC TCTTGCTTCT CAAAGACGCT CAGGTGTTTG GTGAGGAATG GG - #GTTACTCC
720
- AGTGAAGATG TTGCCGAGTT CTACCATAGG CAGCTCAAGT TGACTCAACA GT - #ACACAGAC
780
- CACTGCGTCA ACTGGTACAA CGTTGGGCTC AATGGTCTTA GAGGATCTAC CT - #ACGACGCA
840
- TGGGTGAAGT TCAACAGGTT TCGTAGAGAG ATGACCTTGA CTGTGCTCGA TC - #TTATCGTT
900
- CTCTTTCCAT TCTACGACAT TCGTCTTTAC TCCAAAGGCG TTAAGACAGA GC - #TGACCAGA
960
- GACATCTTCA CCGATCCCAT CTTCTCACTT AACACCCTGC AGGAATACGG TC - #CAACTTTT
1020
- CTCTCCATTG AGAACAGCAT CAGGAAGCCT CACCTCTTCG ACTATCTGCA AG - #GCATTGAG
1080
- TTTCACACCA GGTTGCAACC TGGTTACTTC GGTAAGGATT CCTTCAACTA CT - #GGAGCGGA
1140
- AACTACGTTG AAACCAGACC ATCCATCGGA TCTAGCAAGA CCATCACTTC TC - #CATTCTAC
1200
- GGTGACAAGA GCACTGAGCC AGTGCAGAAG TTGAGCTTCG ATGGGCAGAA GG - #TGTATAGA
1260
- ACCATCGCCA ATACCGATGT TGCAGCTTGG CCTAATGGCA AGGTCTACCT TG - #GAGTTACT
1320
- AAAGTGGACT TCTCCCAATA CGACGATCAG AAGAACGAGA CATCTACTCA AA - #CCTACGAT
1380
- AGTAAGAGGA ACAATGGCCA TGTTTCCGCA CAAGACTCCA TTGACCAACT TC - #CACCTGAA
1440
- ACCACTGATG AACCATTGGA GAAGGCTTAC AGTCACCAAC TTAACTACGC CG - #AATGCTTT
1500
- CTCATGCAAG ACAGGCGTGG CACCATTCCG TTCTTTACAT GGACTCACAG GT - #CTGTCGAC
1560
- TTCTTTAACA CTATCGACGC TGAGAAGATT ACCCAACTTC CCGTGGTCAA GG - #CTTATGCC
1620
- TTGTCCAGCG GAGCTTCCAT CATTGAAGGT CCAGGCTTCA CCGGTGGCAA CT - #TGCTCTTC
1680
- CTTAAGGAGT CCAGCAACTC CATCGCCAAG TTCAAAGTGA CACTTAACTC AG - #CAGCCTTG
1740
- CTCCAACGTT ACAGGGTTCG TATCAGATAC GCAAGCACTA CCAATCTTCG CC - #TCTTTGTC
1800
- CAGAACAGCA ACAATGATTT CCTTGTCATC TACATCAACA AGACTATGAA CA - #AAGACGAT
1860
- GACCTCACCT ACAACACATT CGATCTTGCC ACTACCAATA GTAACATGGG AT - #TCTCTGGT
1920
- GACAAGAACG AGCTGATCAT AGGTGCTGAG AGCTTTGTCT CTAATGAGAA GA - #TTTACATA
1980
- GACAAGATCG AGTTCATTCC AGTTCAACTC TAATAGATCC CCCGGGCTGC AG - #GAATTCGA
2040
# 2050
- (2) INFORMATION FOR SEQ ID NO:102:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 2280 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:102:
- TTAAAATTAA TTTTGTATAC TTTTCATTGT AATAATATGA TTTTAAAAAC GA - #AAAAGTGC
60
- ATATACAACT TATCAGGAGG GGGGGGATGC ACAAAGAAGA AAAGAATAAG AA - #GTGAATGT
120
- TTATAATGTT CAATAGTTTT ATGGGAAGGC ATTTTATCAG GTAGAAAGTT AT - #GTATTATG
180
- ATAAGAATGG GAGGAAGAAA AATGAATCCA AACAATCGAA GTGAACATGA TA - #CGATAAAG
240
- GTTACACCTA ACAGTGAATT GCAAACTAAC CATAATCAAT ATCCTTTAGC TG - #ACAATCCA
300
- AATTCAACAC TAGAAGAATT AAATTATAAA GAATTTTTAA GAATGACTGA AG - #ACAGTTCT
360
- ACGGAAGTGC TAGACAACTC TACAGTAAAA GATGCAGTTG GGACAGGAAT TT - #CTGTTGTA
420
- GGGCAGATTT TAGGTGTTGT AGGAGTTCCA TTTGCTGGGG CACTCACTTC AT - #TTTATCAA
480
- TCATTTCTTA ACACTATATG GCCAAGTGAT GCTGACCCAT GGAAGGCTTT TA - #TGGCACAA
540
- GTTGAAGTAC TGATAGATAA GAAAATAGAG GAGTATGCTA AAAGTAAAGC TC - #TTGCAGAG
600
- TTACAGGGTC TTCAAAATAA TTTCGAAGAT TATGTTAATG CGTTAAATTC CT - #GGAAGAAA
660
- ACACCTTTAA GTTTGCGAAG TAAAAGAAGC CAAGATCGAA TAAGGGAACT TT - #TTTCTCAA
720
- GCAGAAAGTC ATTTTCGTAA TTCCATGCCG TCATTTGCAG TTTCCAAATT CG - #AAGTGCTG
780
- TTTCTACCAA CATATGCACA AGCTGCAAAT ACACATTTAT TGCTATTAAA AG - #ATGCTCAA
840
- GTTTTTGGAG AAGAATGGGG ATATTCTTCA GAAGATGTTG CTGAATTTTA TC - #ATAGACAA
900
- TTAAAACTTA CACAACAATA CACTGACCAT TGTGTTAATT GGTATAATGT TG - #GATTAAAT
960
- GGTTTAAGAG GTTCAACTTA TGATGCATGG GTCAAATTTA ACCGTTTTCG CA - #GAGAAATG
1020
- ACTTTAACTG TATTAGATCT AATTGTACTT TTCCCATTTT ATGATATTCG GT - #TATACTCA
1080
- AAAGGGGTTA AAACAGAACT AACAAGAGAC ATTTTTACGG ATCCAATTTT TT - #CACTTAAT
1140
- ACTCTTCAGG AGTATGGACC AACTTTTTTG AGTATAGAAA ACTCTATTCG AA - #AACCTCAT
1200
- TTATTTGATT ATTTACAGGG GATTGAATTT CATACGCGTC TTCAACCTGG TT - #ACTTTGGG
1260
- AAAGATTCTT TCAATTATTG GTCTGGTAAT TATGTAGAAA CTAGACCTAG TA - #TAGGATCT
1320
- AGTAAGACAA TTACTTCCCC ATTTTATGGA GATAAATCTA CTGAACCTGT AC - #AAAAGCTA
1380
- AGCTTTGATG GACAAAAAGT TTATCGAACT ATAGCTAATA CAGACGTAGC GG - #CTTGGCCG
1440
- AATGGTAAGG TATATTTAGG TGTTACGAAA GTTGATTTTA GTCAATATGA TG - #ATCAAAAA
1500
- AATGAAACTA GTACACAAAC ATATGATTCA AAAAGAAACA ATGGCCATGT AA - #GTGCACAG
1560
- GATTCTATTG ACCAATTACC GCCAGAAACA ACAGATGAAC CACTTGAAAA AG - #CATATAGT
1620
- CATCAGCTTA ATTACGCGGA ATGTTTCTTA ATGCAGGACC GTCGTGGAAC AA - #TTCCATTT
1680
- TTTACTTGGA CACATAGAAG TGTAGACTTT TTTAATACAA TTGATGCTGA AA - #AGATTACT
1740
- CAACTTCCAG TAGTGAAAGC ATATGCCTTG TCTTCAGGTG CTTCCATTAT TG - #AAGGTCCA
1800
- GGATTCACAG GAGGAAATTT ACTATTCCTA AAAGAATCTA GTAATTCAAT TG - #CTAAATTT
1860
- AAAGTTACAT TAAATTCAGC AGCCTTGTTA CAACGATATC GTGTAAGAAT AC - #GCTATGCT
1920
- TCTACCACTA ACTTACGACT TTTTGTGCAA AATTCAAACA ATGATTTTCT TG - #TCATCTAC
1980
- ATTAATAAAA CTATGAATAA AGATGATGAT TTAACATATC AAACATTTGA TC - #TCGCAACT
2040
- ACTAATTCTA ATATGGGGTT CTCGGGTGAT AAGAATGAAC TTATAATAGG AG - #CAGAATCT
2100
- TTCGTTTCTA ATGAAAAAAT CTATATAGAT AAGATAGAAT TTATCCCAGT AC - #AATTGTAA
2160
- GGAGATTTTA AAATGTTGGG TGATGGTCAA AATGAAAGAA TAGGAAGGTG AA - #TTTTGATG
2220
- GTTAGGAAAG ATTCTTTTAA CAAAAGCAAC ATGGAAAAGT ATACAGTACA AA - #TATTAACC
2280
- (2) INFORMATION FOR SEQ ID NO:103:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 32 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:103:
# 32 GCAA ACCCTAACAA TC
- (2) INFORMATION FOR SEQ ID NO:104:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 42 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:104:
# 42 ACGA CCCTGCAGAA ATACGGTCCA AC
- (2) INFORMATION FOR SEQ ID NO:105:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 28 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:105:
# 28 CATT CGATCTTG
- (2) INFORMATION FOR SEQ ID NO:106:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 25 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:106:
# 25 CAGC TCAAG
- (2) INFORMATION FOR SEQ ID NO:107:
- (i) SEQUENCE CHARACTERISTICS:
#pairs (A) LENGTH: 1959 base
(B) TYPE: nucleic acid
(C) STRANDEDNESS: single
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:107:
- ATGAATCCAA ACAATCGAAG TGAACATGAT ACGATAAAGG TTACACCTAA CA - #GTGAATTG
60
- CAAACTAACC ATAATCAATA TCCTTTAGCT GACAATCCAA ATTCAACACT AG - #AAGAATTA
120
- AATTATAAAG AATTTTTAAG AATGACTGAA GACAGTTCTA CGGAAGTGCT AG - #ACAACTCT
180
- ACAGTAAAAG ATGCAGTTGG GACAGGAATT TCTGTTGTAG GGCAGATTTT AG - #GTGTTGTA
240
- GGAGTTCCAT TTGCTGGGGC ACTCACTTCA TTTTATCAAT CATTTCTTAA CA - #CTATATGG
300
- CCAAGTGATG CTGACCCATG GAAGGCTTTT ATGGCACAAG TTGAAGTACT GA - #TAGATAAG
360
- AAAATAGAGG AGTATGCTAA AAGTAAAGCT CTTGCAGAGT TACAGGGTCT TC - #AAAATAAT
420
- TTCGAAGATT ATGTTAATGC GTTAAATTCC TGGAAGAAAA CACCTTTAAG TT - #TGCGAAGT
480
- AAAAGAAGCC AAGGTCGAAT AAGGGAACTT TTTTCTCAAG CAGAAAGTCA TT - #TTCGTAAT
540
- TCCATGCCGT CATTTGCAGT TTCCAAATTC GAAGTGCTGT TTCTACCAAC AT - #ATGCACAA
600
- GCTGCAAATA CACATTTATT GCTATTAAAA GATGCTCAAG TTTTTGGAGA AG - #AATGGGGA
660
- TATTCTTCAG AAGATGTTGC TGAATTCTAT CGTAGACAAT TAAAACTTAC AC - #AACAATAC
720
- ACTGACCATT GTGTTAATTG GTATAATGTT GGATTAAATG GTTTAAGAGG TT - #CAACTTAT
780
- GATGCATGGG TCAAATTTAA CCGTTTTCGC AGAGAAATGA CTTTAACTGT AT - #TAGATCTA
840
- ATTGTACTTT TCCCATTTTA TGATATTCGG TTATACTCAA AAGGGGTTAA AA - #CAGAACTA
900
- ACAAGAGACA TTTTTACGGA TCCAATTTTT TTACTTACTA CGCTTCAGAA GT - #ACGGACCA
960
- ACTTTTTTGA GTATAGAAAA CTCTATTCGA AAACCTCATT TATTTGATTA TT - #TACAGGGG
1020
- ATTGAATTTC ATACGCGTCT TCAACCTGGT TACTTTGGGA AAGATTCTTT CA - #ATTATTGG
1080
- TCTGGTAATT ATGTAGAAAC TAGACCTAGT ATAGGATCTA GTAAGACAAT TA - #CTTCCCCA
1140
- TTTTATGGAG ATAAATCTAC TGAACCTGTA CAAAAGCTAA GCTTTGATGG AC - #AAAAAGTT
1200
- TATCGAACTA TAGCTAATAC AGACGTAGCG GCTTGGCCGA ATGGTAAGGT AT - #ATTTAGGT
1260
- GTTACGAAAG TTGATTTTAG TCAATATGAT GATCAAAAAA ATGAAACTAG TA - #CACAAACA
1320
- TATGATTCAA AAAGAAACAA TGGCCATGTA AGTGCACAGG ATTCTATTGA CC - #AATTACCG
1380
- CCAGAAACAA CAGATGAACC ACTTGAAAAA GCATATAGTC ATCAGCTTAA TT - #ACGCGGAA
1440
- TGTTTCTTAA TGCAGGACCG TCGTGGAACA ATTCCATTTT TTACTTGGAC AC - #ATAGAAGT
1500
- GTAGACTTTT TTAATACAAT TGATGCTGAA AAGATTACTC AACTTCCAGT AG - #TGAAAGCA
1560
- TATGCCTTGT CTTCAGGTGC TTCCATTATT GAAGGTCCAG GATTCACAGG AG - #GAAATTTA
1620
- CTATTCCTAA AAGAATCTAG TAATTCAATT GCTAAATTTA AAGTTACATT AA - #ATTCAGCA
1680
- GCCTTGTTAC AACGATATCG TGTAAGAATA CGCTATGCTT CTACCACTAA CT - #TACGACTT
1740
- TTTGTGCAAA ATTCAAACAA TGATTTTCTT GTCATCTACA TTAATAAAAC TA - #TGAATAAA
1800
- GATGATGATT TAACATATCA AACATTTGAT CTCGCAACTA CTAATTCTAA TA - #TGGGGTTC
1860
- TCGGGTGATA AGAATGAACT TATAATAGGA GCAGAATCTT TCGTTTCTAA TG - #AAAAAATC
1920
# 1959 AATT TATCCCAGTA CAATTGTAA
- (2) INFORMATION FOR SEQ ID NO:108:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:108:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
#80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Gly Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr Arg Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Leu Leu Thr Thr Le - #u Gln Lys Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:109:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 649 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:109:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Ala Thr Glu
# 15
- Asn Asn Glu Val Ser Asn Asn His Ala Gln Ty - #r Pro Leu Ala Asp Thr
# 30
- Pro Thr Leu Glu Glu Leu Asn Tyr Lys Glu Ph - #e Leu Arg Arg Thr Thr
# 45
- Asp Asn Asn Val Glu Ala Leu Asp Ser Ser Th - #r Thr Lys Asp Ala Ile
# 60
- Gln Lys Gly Ile Ser Ile Ile Gly Asp Leu Le - #u Gly Val Val Gly Phe
#80
- Pro Tyr Gly Gly Ala Leu Val Ser Phe Tyr Th - #r Asn Leu Leu Asn Thr
# 95
- Ile Trp Pro Gly Glu Asp Pro Leu Lys Ala Ph - #e Met Gln Gln Val Glu
# 110
- Ala Leu Ile Asp Gln Lys Ile Ala Asp Tyr Al - #a Lys Asp Lys Ala Thr
# 125
- Ala Glu Leu Gln Gly Leu Lys Asn Val Phe Ly - #s Asp Tyr Val Ser Ala
# 140
- Leu Asp Ser Trp Asp Lys Thr Pro Leu Thr Le - #u Arg Asp Gly Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Gln Gly Arg Ile Arg Glu Leu Phe Ser Gln Al - #a Glu Ser His Phe Arg
# 175
- Arg Ser Met Pro Ser Phe Ala Val Ser Gly Ty - #r Glu Val Leu Phe Leu
# 190
- Pro Thr Tyr Ala Gln Ala Ala Asn Thr His Le - #u Leu Leu Leu Lys Asp
# 205
- Ala Gln Ile Tyr Gly Thr Asp Trp Gly Tyr Se - #r Thr Asp Asp Leu Asn
# 220
- Glu Phe His Thr Lys Gln Lys Asp Leu Thr Il - #e Glu Tyr Thr Asn His
225 2 - #30 2 - #35 2 -
#40
- Cys Ala Lys Trp Tyr Lys Ala Gly Leu Asp Ly - #s Leu Arg Gly Ser Thr
# 255
- Tyr Glu Glu Trp Val Lys Phe Asn Arg Tyr Ar - #g Arg Glu Met Thr Leu
# 270
- Thr Val Leu Asp Leu Ile Thr Leu Phe Pro Le - #u Tyr Asp Val Arg Thr
# 285
- Tyr Thr Lys Gly Val Lys Thr Glu Leu Thr Ar - #g Asp Val Leu Thr Asp
# 300
- Pro Ile Val Ala Val Asn Asn Met Asn Gly Ty - #r Gly Thr Thr Phe Ser
305 3 - #10 3 - #15 3 -
#20
- Asn Ile Glu Asn Tyr Ile Arg Lys Pro His Le - #u Phe Asp Tyr Leu His
# 335
- Ala Ile Gln Phe His Ser Arg Leu Gln Pro Gl - #y Tyr Phe Gly Thr Asp
# 350
- Ser Phe Asn Tyr Trp Ser Gly Asn Tyr Val Se - #r Thr Arg Ser Ser Ile
# 365
- Gly Ser Asp Glu Ile Ile Arg Ser Pro Phe Ty - #r Gly Asn Lys Ser Thr
# 380
- Leu Asp Val Gln Asn Leu Glu Phe Asn Gly Gl - #u Lys Val Phe Arg Ala
385 3 - #90 3 - #95 4 -
#00
- Val Ala Asn Gly Asn Leu Ala Val Trp Pro Va - #l Gly Thr Gly Gly Thr
# 415
- Lys Ile His Ser Gly Val Thr Lys Val Gln Ph - #e Ser Gln Tyr Asn Asp
# 430
- Arg Lys Asp Glu Val Arg Thr Gln Thr Tyr As - #p Ser Lys Arg Asn Val
# 445
- Gly Gly Ile Val Phe Asp Ser Ile Asp Gln Le - #u Pro Pro Ile Thr Thr
# 460
- Asp Glu Ser Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Val Arg
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Leu Gln Gly Gly Arg Gly Ile Il - #e Pro Val Phe Thr Trp
# 495
- Thr His Lys Ser Val Asp Phe Tyr Asn Thr Le - #u Asp Ser Glu Lys Ile
# 510
- Thr Gln Ile Pro Phe Val Lys Ala Phe Ile Le - #u Val Asn Ser Thr Ser
# 525
- Val Val Ala Gly Pro Gly Phe Thr Gly Gly As - #p Ile Ile Lys Cys Thr
# 540
- Asn Gly Ser Gly Leu Thr Leu Tyr Val Thr Pr - #o Ala Pro Asp Leu Thr
545 5 - #50 5 - #55 5 -
#60
- Tyr Ser Lys Thr Tyr Lys Ile Arg Ile Arg Ty - #r Ala Ser Thr Ser Gln
# 575
- Val Arg Phe Gly Ile Asp Leu Gly Ser Tyr Th - #r His Ser Ile Ser Tyr
# 590
- Phe Asp Lys Thr Met Asp Lys Gly Asn Thr Le - #u Thr Tyr Asn Ser Phe
# 605
- Asn Leu Ser Ser Val Ser Arg Pro Ile Glu Il - #e Ser Gly Gly Asn Lys
# 620
- Ile Gly Val Ser Val Gly Gly Ile Gly Ser Gl - #y Asp Glu Val Tyr Ile
625 6 - #30 6 - #35 6 -
#40
- Asp Lys Ile Glu Phe Ile Pro Met Asp
645
- (2) INFORMATION FOR SEQ ID NO:110:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:110:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Pro Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
#80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asp Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Val Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Ser
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Ile Tyr Phe Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Gly Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Ile Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Ile Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Thr
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:111:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:111:
- Met Asn Pro Asn Asn Arg Ser Glu His Asp Th - #r Ile Lys Val Thr Pro
# 15
- Asn Ser Glu Leu Gln Thr Asn His Asn Gln Ty - #r Pro Leu Ala Asp Asn
# 30
- Pro Asn Ser Thr Leu Glu Glu Leu Asn Tyr Ly - #s Glu Phe Leu Arg Met
# 45
- Thr Glu Asp Ser Ser Thr Glu Val Leu Asp As - #n Ser Thr Val Lys Asp
# 60
- Ala Val Gly Thr Gly Ile Ser Val Val Gly Gl - #n Ile Leu Gly Val Val
#80
- Gly Val Pro Phe Ala Gly Ala Leu Thr Ser Ph - #e Tyr Gln Ser Phe Leu
# 95
- Asn Thr Ile Trp Pro Ser Asp Ala Asp Pro Tr - #p Lys Ala Phe Met Ala
# 110
- Gln Val Glu Val Leu Ile Asp Lys Lys Ile Gl - #u Glu Tyr Ala Lys Ser
# 125
- Lys Ala Leu Ala Glu Leu Gln Gly Leu Gln As - #n Asn Phe Glu Asp Tyr
# 140
- Val Asn Ala Leu Asn Ser Trp Lys Lys Thr Pr - #o Leu Ser Leu Arg Ser
145 1 - #50 1 - #55 1 -
#60
- Lys Arg Ser Gln Asp Arg Ile Arg Glu Leu Ph - #e Ser Gln Ala Glu Ser
# 175
- His Phe Arg Asn Ser Met Pro Ser Phe Ala Va - #l Ser Lys Phe Glu Val
# 190
- Leu Phe Leu Pro Thr Tyr Ala Gln Ala Ala As - #n Thr His Leu Leu Leu
# 205
- Leu Lys Asp Ala Gln Val Phe Gly Glu Glu Tr - #p Gly Tyr Ser Ser Glu
# 220
- Asp Val Ala Glu Phe Tyr His Arg Gln Leu Ly - #s Leu Thr Gln Gln Tyr
225 2 - #30 2 - #35 2 -
#40
- Thr Asp His Cys Val Asn Trp Tyr Asn Val Gl - #y Leu Asn Gly Leu Arg
# 255
- Gly Ser Thr Tyr Asp Ala Trp Val Lys Phe As - #n Arg Phe Arg Arg Glu
# 270
- Met Thr Leu Thr Val Leu Asp Leu Ile Val Le - #u Phe Pro Phe Tyr Asp
# 285
- Ile Arg Leu Tyr Ser Lys Gly Val Lys Thr Gl - #u Leu Thr Arg Asp Ile
# 300
- Phe Thr Asp Pro Ile Phe Ser Leu Asn Thr Le - #u Gln Glu Tyr Gly Pro
305 3 - #10 3 - #15 3 -
#20
- Thr Phe Leu Ser Ile Glu Asn Ser Ile Arg Ly - #s Pro His Leu Phe Asp
# 335
- Tyr Leu Gln Gly Ile Glu Phe His Thr Arg Le - #u Gln Pro Gly Tyr Phe
# 350
- Gly Lys Asp Ser Phe Asn Tyr Trp Ser Gly As - #n Tyr Val Glu Thr Arg
# 365
- Pro Ser Ile Gly Ser Ser Lys Thr Ile Thr Se - #r Pro Phe Tyr Gly Asp
# 380
- Lys Ser Thr Glu Pro Val Gln Lys Leu Ser Ph - #e Asp Gly Gln Lys Val
385 3 - #90 3 - #95 4 -
#00
- Tyr Arg Thr Ile Ala Asn Thr Asp Val Ala Al - #a Trp Pro Asn Gly Lys
# 415
- Val Tyr Leu Gly Val Thr Lys Val Asp Phe Se - #r Gln Tyr Asp Asp Gln
# 430
- Lys Asn Glu Thr Ser Thr Gln Thr Tyr Asp Se - #r Lys Arg Asn Asn Gly
# 445
- His Val Ser Ala Gln Asp Ser Ile Asp Gln Le - #u Pro Pro Glu Thr Thr
# 460
- Asp Glu Pro Leu Glu Lys Ala Tyr Ser His Gl - #n Leu Asn Tyr Ala Glu
465 4 - #70 4 - #75 4 -
#80
- Cys Phe Leu Met Gln Asp Arg Arg Gly Thr Il - #e Pro Phe Phe Thr Trp
# 495
- Thr His Arg Ser Val Asp Phe Phe Asn Thr Il - #e Asp Ala Glu Lys Ile
# 510
- Thr Gln Leu Pro Val Val Lys Ala Tyr Ala Le - #u Ser Ser Gly Ala Ser
# 525
- Ile Ile Glu Gly Pro Gly Phe Thr Gly Gly As - #n Leu Leu Phe Leu Lys
# 540
- Glu Ser Ser Asn Ser Ile Ala Lys Phe Lys Va - #l Thr Leu Asn Ser Ala
545 5 - #50 5 - #55 5 -
#60
- Ala Leu Leu Gln Arg Tyr Arg Val Arg Ile Ar - #g Tyr Ala Ser Thr Thr
# 575
- Asn Leu Arg Leu Phe Val Gln Asn Ser Asn As - #n Asp Phe Leu Val Ile
# 590
- Tyr Ile Asn Lys Thr Met Asn Lys Asp Asp As - #p Leu Thr Tyr Gln Thr
# 605
- Phe Asp Leu Ala Thr Thr Asn Ser Asn Met Gl - #y Phe Ser Gly Asp Lys
# 620
- Asn Glu Leu Ile Ile Gly Ala Glu Ser Phe Va - #l Ser Asn Glu Lys Ile
625 6 - #30 6 - #35 6 -
#40
- Tyr Ile Asp Lys Ile Glu Phe Ile Pro Val Gl - #n Leu
# 650
- (2) INFORMATION FOR SEQ ID NO:112:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 659 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:112:
- Met Ile Arg Met Gly Gly Arg Lys Met Asn Pr - #o Asn Asn Arg Ser Glu
# 15
- Tyr Asp Thr Ile Lys Val Thr Pro Asn Ser Gl - #u Leu Pro Thr Asn His
# 30
- Asn Gln Tyr Pro Leu Ala Asp Asn Pro Asn Se - #r Thr Leu Glu Glu Leu
# 45
- Asn Tyr Lys Glu Phe Leu Arg Met Thr Ala As - #p Asn Ser Thr Glu Val
# 60
- Leu Asp Ser Ser Thr Val Lys Asp Ala Val Gl - #y Thr Gly Ile Ser Val
#80
- Val Gly Gln Ile Leu Gly Val Val Gly Val Pr - #o Phe Ala Gly Ala Leu
# 95
- Thr Ser Phe Tyr Gln Ser Phe Leu Asn Ala Il - #e Trp Pro Ser Asp Ala
# 110
- Asp Pro Trp Lys Ala Phe Met Ala Gln Val Gl - #u Val Leu Ile Asp Lys
# 125
- Lys Ile Glu Glu Tyr Ala Lys Ser Lys Ala Le - #u Ala Glu Leu Gln Gly
# 140
- Leu Gln Asn Asn Phe Glu Asp Tyr Val Asn Al - #a Leu Asp Ser Trp Lys
145 1 - #50 1 - #55 1 -
#60
- Lys Ala Pro Val Asn Leu Arg Ser Arg Arg Se - #r Gln Asp Arg Ile Arg
# 175
- Glu Leu Phe Ser Gln Ala Glu Ser His Phe Ar - #g Asn Ser Met Pro Ser
# 190
- Phe Ala Val Ser Lys Phe Glu Val Leu Phe Le - #u Pro Thr Tyr Ala Gln
# 205
- Ala Ala Asn Thr His Leu Leu Leu Leu Lys As - #p Ala Gln Val Phe Gly
# 220
- Glu Glu Trp Gly Tyr Ser Ser Glu Asp Ile Al - #a Glu Phe Tyr Gln Arg
225 2 - #30 2 - #35 2 -
#40
- Gln Leu Lys Leu Thr Gln Gln Tyr Thr Asp Hi - #s Cys Val Asn Trp Tyr
# 255
- Asn Val Gly Leu Asn Ser Leu Arg Gly Ser Th - #r Tyr Asp Ala Trp Val
# 270
- Lys Phe Asn Arg Phe Arg Arg Glu Met Thr Le - #u Thr Val Leu Asp Leu
# 285
- Ile Val Leu Phe Pro Phe Tyr Asp Val Arg Le - #u Tyr Ser Lys Gly Val
# 300
- Lys Thr Glu Leu Thr Arg Asp Ile Phe Thr As - #p Pro Ile Phe Thr Leu
305 3 - #10 3 - #15 3 -
#20
- Asn Ala Leu Gln Glu Tyr Gly Pro Thr Phe Se - #r Ser Ile Glu Asn Ser
# 335
- Ile Arg Lys Pro His Leu Phe Asp Tyr Leu Ar - #g Gly Ile Glu Phe His
# 350
- Thr Arg Leu Arg Pro Gly Tyr Ser Gly Lys As - #p Ser Phe Asn Tyr Trp
# 365
- Ser Gly Asn Tyr Val Glu Thr Arg Pro Ser Il - #e Gly Ser Asn Asp Thr
# 380
- Ile Thr Ser Pro Phe Tyr Gly Asp Lys Ser Il - #e Glu Pro Ile Gln Lys
385 3 - #90 3 - #95 4 -
#00
- Leu Ser Phe Asp Gly Gln Lys Val Tyr Arg Th - #r Ile Ala Asn Thr Asp
# 415
- Ile Ala Ala Phe Pro Asp Gly Lys Ile Tyr Ph - #e Gly Val Thr Lys Val
# 430
- Asp Phe Ser Gln Tyr Asp Asp Gln Lys Asn Gl - #u Thr Ser Thr Gln Thr
# 445
- Tyr Asp Ser Lys Arg Tyr Asn Gly Tyr Leu Gl - #y Ala Gln Asp Ser Ile
# 460
- Asp Gln Leu Pro Pro Glu Thr Thr Asp Glu Pr - #o Leu Glu Lys Ala Tyr
465 4 - #70 4 - #75 4 -
#80
- Ser His Gln Leu Asn Tyr Ala Glu Cys Phe Le - #u Met Gln Asp Arg Arg
# 495
- Gly Thr Ile Pro Phe Phe Thr Trp Thr His Ar - #g Ser Val Asp Phe Phe
# 510
- Asn Thr Ile Asp Ala Glu Lys Ile Thr Gln Le - #u Pro Val Val Lys Ala
# 525
- Tyr Ala Leu Ser Ser Gly Ala Ser Ile Ile Gl - #u Gly Pro Gly Phe Thr
# 540
- Gly Gly Asn Leu Leu Phe Leu Lys Glu Ser Se - #r Asn Ser Ile Ala Lys
545 5 - #50 5 - #55 5 -
#60
- Phe Lys Val Thr Leu Asn Ser Ala Ala Leu Le - #u Gln Arg Tyr Arg Val
# 575
- Arg Ile Arg Tyr Ala Ser Thr Thr Asn Leu Ar - #g Leu Phe Val Gln Asn
# 590
- Ser Asn Asn Asp Phe Leu Val Ile Tyr Ile As - #n Lys Thr Met Asn Ile
# 605
- Asp Gly Asp Leu Thr Tyr Gln Thr Phe Asp Ph - #e Ala Thr Ser Asn Ser
# 620
- Asn Met Gly Phe Ser Gly Asp Thr Asn Asp Ph - #e Ile Ile Gly Ala Glu
625 6 - #30 6 - #35 6 -
#40
- Ser Phe Val Ser Asn Glu Lys Ile Tyr Ile As - #p Lys Ile Glu Phe Ile
# 655
- Pro Val Gln
- (2) INFORMATION FOR SEQ ID NO:113:
- (i) SEQUENCE CHARACTERISTICS:
#acids (A) LENGTH: 652 amino
(B) TYPE: amino acid
(C) STRANDEDNESS:
(D) TOPOLOGY: linear
- (xi) SEQUENCE DESCRIPTION: SEQ ID NO:113:
- Met Ile Arg Lys Gly Gly Arg Lys Met Asn Pr - #o Asn Asn Arg Ser Glu
# 15
- His Asp Thr Ile Lys Thr Thr Glu Asn Asn Gl - #u Val Pro Thr Asn His
# 30
- Val Gln Tyr Pro Leu Ala Glu Thr Pro Asn Pr - #o Thr Leu Glu Asp Leu
# 45
- Asn Tyr Lys Glu Phe Leu Arg Met Thr Ala As - #p Asn Asn Thr Glu Ala
# 60
- Leu Asp Ser Ser Thr Thr Lys Asp Val Ile Gl - #n Lys Gly Ile Ser Val
#80
- Val Gly Asp Leu Leu Gly Val Val Gly Phe Pr - #o Phe Gly Gly Ala Leu
# 95
- Val Ser Phe Tyr Thr Asn Phe Leu Asn Thr Il - #e Trp Pro Ser Glu Asp
# 110
- Pro Trp Lys Ala Phe Met Glu Gln Val Glu Al - #a Leu Met Asp Gln Lys
# 125
- Ile Ala Asp Tyr Ala Lys Asn Lys Ala Leu Al - #a Glu Leu Gln Gly Leu
# 140
- Gln Asn Asn Val Glu Asp Tyr Val Ser Ala Le - #u Ser Ser Trp Gln Lys
145 1 - #50 1 - #55 1 -
#60
- Asn Pro Val Ser Ser Arg Asn Pro His Ser Gl - #n Gly Arg Ile Arg Glu
# 175
- Leu Phe Ser Gln Ala Glu Ser His Phe Arg As - #n Ser Met Pro Ser Phe
# 190
- Ala Ile Ser Gly Tyr Glu Val Leu Phe Leu Th - #r Thr Tyr Ala Gln Ala
# 205
- Ala Asn Thr His Leu Phe Leu Leu Lys Asp Al - #a Gln Ile Tyr Gly Glu
# 220
- Glu Trp Gly Tyr Glu Lys Glu Asp Ile Ala Gl - #u Phe Tyr Lys Arg Gln
225 2 - #30 2 - #35 2 -
#40
- Leu Lys Leu Thr Gln Glu Tyr Thr Asp His Cy - #s Val Lys Trp Tyr Asn
# 255
- Val Gly Leu Asp Lys Leu Arg Gly Ser Ser Ty - #r Glu Ser Trp Val Asn
# 270
- Phe Asn Arg Tyr Arg Arg Glu Met Thr Leu Th - #r Val Leu Asp Leu Ile
# 285
- Ala Leu Phe Pro Leu Tyr Asp Val Arg Leu Ty - #r Pro Lys Glu Val Lys
# 300
- Thr Glu Leu Thr Arg Asp Val Leu Thr Asp Pr - #o Ile Val Gly Val Asn
305 3 - #10 3 - #15 3 -
#20
- Asn Leu Arg Gly Tyr Gly Thr Thr Phe Ser As - #n Ile Glu Asn Tyr Ile
# 335
- Arg Lys Pro His Leu Phe Asp Tyr Leu His Ar - #g Ile Gln Phe His Thr
# 350
- Arg Phe Gln Pro Gly Tyr Tyr Gly Asn Asp Se - #r Phe Asn Tyr Trp Ser
# 365
- Gly Asn Tyr Val Ser Thr Arg Pro Ser Ile Gl - #y Ser Asn Asp Ile Ile
# 380
- Thr Ser Pro Phe Tyr Gly Asn Lys Ser Ser Gl - #u Pro Val Gln Asn Leu
385 3 - #90 3 - #95 4 -
#00
- Glu Phe Asn Gly Glu Lys Val Tyr Arg Ala Va - #l Ala Asn Thr Asn Leu
# 415
- Ala Val Trp Pro Ser Ala Val Tyr Ser Gly Va - #l Thr Lys Val Glu Phe
# 430
- Ser Gln Tyr Asn Asp Gln Thr Asp Glu Ala Se - #r Thr Gln Thr Tyr Asp
# 445
- Ser Lys Arg Asn Val Gly Ala Val Ser Trp As - #p Ser Ile Asp Gln Leu
# 460
- Pro Pro Glu Thr Thr Asp Glu Pro Leu Glu Ly - #s Gly Tyr Ser His Gln
465 4 - #70 4 - #75 4 -
#80
- Leu Asn Tyr Val Met Cys Phe Leu Met Gln Gl - #y Ser Arg Gly Thr Ile
# 495
- Pro Val Leu Thr Trp Thr His Lys Ser Val As - #p Phe Phe Asn Met Ile
# 510
- Asp Ser Lys Lys Ile Thr Gln Leu Pro Leu Va - #l Lys Ala Tyr Lys Leu
# 525
- Gln Ser Gly Ala Ser Val Val Ala Gly Pro Ar - #g Phe Thr Gly Gly Asp
# 540
- Ile Ile Gln Cys Thr Glu Asn Gly Ser Ala Al - #a Thr Ile Tyr Val Thr
545 5 - #50 5 - #55 5 -
#60
- Pro Asp Val Ser Tyr Ser Gln Lys Tyr Arg Al - #a Arg Ile His Tyr Ala
# 575
- Ser Thr Ser Gln Ile Thr Phe Thr Leu Ser Le - #u Asp Gly Ala Pro Phe
# 590
- Asn Gln Tyr Tyr Phe Asp Lys Thr Ile Asn Ly - #s Gly Asp Thr Leu Thr
# 605
- Tyr Asn Ser Phe Asn Leu Ala Ser Phe Ser Th - #r Pro Phe Glu Leu Ser
# 620
- Gly Asn Asn Leu Gln Ile Gly Val Thr Gly Le - #u Ser Ala Gly Asp Lys
625 6 - #30 6 - #35 6 -
#40
- Val Tyr Ile Asp Lys Ile Glu Phe Ile Pro Va - #l Asn
# 650
__________________________________________________________________________
Claims (41)
1. A method for producing a modified Cry3* polypeptide having improved insecticidal activity or specificity, comprising:
(a) obtaining a three-dimensional crystal structure of a Cry3 polypeptide;
(b) locating in said crystal structure of said Cry3 polypeptide one or more regions of bound water, wherein said bound water forms a contiguous hydrated surface separated by no more than about 16 Å;
(c) increasing the hydrophobicity of one or more amino acids of said Cry3 polypeptide in one or more of said regions; and
(d) obtaining the modified Cry3* polypeptide so produced.
2. The method of claim 1, wherein said modified Cry3* polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:14, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, and SEQ ID NO:54.
3. A method for producing a modified Cry3B* polypeptide having improved insecticidal activity, or enhanced insecticidal specificity, comprising
(a) obtaining a three-dimensional crystal structure of a Cry3B polypeptide;
(b) identifying a loop region in said Cry3B polypeptide;
(c) modifying one or more amino acids in said loop region of said Cry3B polypeptide to increase by hydrophobicity of one or more of said amino acids; and
(d) obtaining the modified Cry3B* polypeptide so produced.
4. The method of claim 3, wherein said modified Cry3B* polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:26, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, and SEQ ID NO:42.
5. A method for increasing the mobility of channel forming helices of a Cry3 polypeptide, comprising disrupting one or more hydrogen bonds formed between a first amino acid of one of said channel forming helices and a second amino acid of said polypeptide, wherein said disrupting comprises replacing said first amino acid or said second amino acid with a third amino acid whose spatial distance bond angle is greater than about 3 Å, or whose spatial orientation is not equal to 180±60 degrees relative to the hydrogen bonding site of said first or said second amino acid.
6. The method of claim 5, wherein said polypeptide having one or more disrupted hydrogen bonds comprises an amino acid sequence selected from the group consisting of SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:22, SEQ ID NO:40, and SEQ ID NO:42.
7. A method for increasing the flexibility of a loop region in a channel forming domain of a Cry3 polypeptide, comprising:
(a) obtaining a crystal structure of a Cry3 polypeptide having a loop region between adjacent α-helices;
(b) identifying the amino acids comprising said loop region;
(c) altering one or more of said amino acids in said loop region to reduce the steric hindrance in said region, wherein said altering increases flexibility of said loop region in said polypeptide; and
(d) obtaining the polypeptide so produced.
8. The method of claim 7, wherein said polypeptide having an altered loop region comprises an amino acid sequence selected from the group consisting of SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:48, and SEQ ID NO:54.
9. A method of increasing the insecticidal activity of a Cry3B polypeptide, comprising reducing or eliminating binding of said polypeptide to a carbohydrate in a target insect gut, wherein said reducing or eliminating is accomplished by removal of one or more α-helices of domain 1 of said Cry3B polypeptide.
10. The method claim 9, wherein said reducing or eliminating is accomplished by removal of α-helices α1, α2a/b, or α3.
11. The method of claim 10, wherein said Cry3B polypeptide comprises the amino acid sequence of SEQ ID NO:70.
12. The method of claim 9, wherein said reducing or eliminating is accomplished by replacing one or more amino acids within loop β1,α8, with one or more amino acids having increased hydrophobicity.
13. The method of claim 12, wherein said Cry3B polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:16, SEQ ID NO:20, SEQ ID NO:22, and SEQ ID NO:34.
14. The method of claim 9, wherein said reducing or eliminating is accomplished by replacing with any other amino acid, one or more amino acids selected from the group consisting of threonine 154, proline 155, leucine 156, and leucine 158.
15. The method of claim 14, wherein said Cry3B polypeptide comprises the amino acid sequence of SEQ ID NO:2.
16. A method of preparing a modified Cry3* polypeptide having improved insecticidal activity or enhanced insecticidal specificity when compared to an unmodified Cry3 polypeptide, said method comprising the steps of:
(a) obtaining a crystal structure of a Cry3 polypeptide;
(b) identifying from said crystal structure one or more surface-exposed amino acids in said Cry3 polypeptide;
(c) randomly substituting one or more of said surface-exposed amino acids to obtain a plurality of mutated polypeptides, wherein at least 50% of said mutated polypeptides have diminished insecticidal activity, or reduced insecticidal specificity;
(d) identifying from said plurality of mutated polypeptides a region of said Cry3 polypeptide for targeted mutagenesis; and
(e) mutagenizing said region to obtain said modified Cry3* polypeptide having improved insecticidal activity or enhanced insecticidal specificity.
17. The method of claim 16, further comprising determining the amino acid sequences of a plurality of mutated polypeptides having diminished activity or reduced insecticidal specificity, and identifying one or more amino acid residues required for said activity or specificity.
18. A process for producing a Cry3* polypeptide having improved insecticidal activity, comprising:
(a) obtaining a three-dimensional crystal structure of a Cry3 polypeptide;
(b) determining the electrostatic surface distribution of said Cry3 polypeptide;
(c) identifying at least one region of high electrostatic diversity in said Cry3 polypeptide;
(d) modifying the electrostatic diversity of said region by altering one or more amino acids in said region; and
(e) obtaining the Cry3* polypeptide so produced.
19. The process of claim 18, wherein said electrostatic diversity is decreased relative to the electrostatic diversity of a native Cry3 polypeptide.
20. The process of claim 19, wherein said Cry3* polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:14, SEQ ID NO:40, and SEQ ID NO:42.
21. The process of claim 18, wherein said electrostatic diversity is increased relative to the electrostatic diversity of a native Cry3 polypeptide.
22. The process of claim 21, wherein said Cry3* polypeptide comprises SEQ ID NO:28.
23. A method of producing a Cry3* polypeptide having improved insecticidal activity, comprising:
(a) obtaining a three-dimensional crystal structure of a Cry3 polypeptide;
(b) identifying the presence of one or more metal binding sites in said Cry3 polypeptide;
(c) altering one or more amino acids in one or more of said binding sites of said Cry3 polypeptide; and
(d) obtaining an altered polypeptide, wherein said polypeptide has improved insecticidal activity.
24. The method of claim 23, wherein said altering eliminates metal binding.
25. The method of claim 24, wherein said Cry3* polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:4, SEQ ID NO:8, SEQ ID NO:10, and SEQ ID NO:12.
26. A method of identifying a Cry3B polypeptide having improved channel activity, comprising:
(a) obtaining a mutant Cry3B polypeptide;
(b) determining the rate of channel formation in said mutant polypeptide, and in a wild-type polypeptide;
(c) comparing said characteristics of said mutant polypeptide and said wild-type polypeptide; and
(d) identifying said mutant polypeptide having an increased rate of channel formation compared to said wild-type polypeptide.
27. The method of claim 26, wherein said mutant Cry3B polypeptide comprises an amino acid sequence selected from the group consisting SEQ ID NO:70, SEQ ID NO:46, SEQ ID NO:52, SEQ ID NO:24, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:12, SEQ ID NO:2, SEQ ID NO:42, and SEQ ID NO:20.
28. A method for producing a modified Cry3B polypeptide, having improved insecticidal activity, comprising altering one or more non-surface amino acids located at a point of convergence of two or more loop regions of said Cry3B polypeptide, wherein said altering decreases the mobility of one or more of said loop regions.
29. The method of claim 28, wherein said mobility is determined by comparing the thermal denaturation of said modified protein to a wild-type Cry3B polypeptide.
30. The method of claim 28, wherein said modified Cry3B polypeptide comprises SEQ ID NO:67.
31. The method of claim 28, wherein said modified Cry3B polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:22, and SEQ ID NO:30.
32. A method of improving the insecticidal activity of a Cry3 polypeptide, said method comprising inserting one or more protease sensitive sites into one or more loop regions of domain 1 of said polypeptide.
33. The method of claim 22, wherein said loop region is α3,4.
34. The method of claim 33, wherein said modified Cry3B polypeptide comprises SEQ ID NO:2.
35. A modified Cry3B* polypeptide prepared by a process comprising the steps of:
(a) identifying a Cry3B polypeptide having one or more loop regions between two adjacent α helices;
(b) introducing one or more mutations into at least one of said loop regions; and
(c) obtaining the modified Cry3B* polypeptide so produced.
36. The polypeptide of claim 35, wherein said polypeptide is selected from the group consisting of Cry3Bb-60, Cry3Bb.11221, Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11234, Cry3Bb.11235, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11032, Cry3Bb.11235, Cry3Bb.11036, Cry3Bb.11046, Cry3Bb.11048, Cry3Bb.11051, Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11095, and Cry3Bb.11098.
37. The polypeptide of claim 35, wherein said polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, and SEQ ID NO:108.
38. The polypeptide of claim 37, wherein said polypeptide is encoded by a nucleic acid sequence selected from the group consisting of SEQ ID NO:1, SEQ ID NO:3, SEQ ID NO:5, SEQ ID NO:7, SEQ ID NO:9, SEQ ID NO:11, SEQ ID NO:13, SEQ ID NO:15, SEQ ID NO:17, SEQ ID NO:19, SEQ ID NO:21, SEQ ID NO:23, SEQ ID NO:25, SEQ ID NO:27, SEQ ID NO:29, SEQ ID NO:31, SEQ ID NO:33, SEQ ID NO:35, SEQ ID NO:37, SEQ ID NO:39, SEQ ID NO:41, SEQ ID NO:43, SEQ ID NO:45, SEQ ID NO:47, SEQ ID NO:49, SEQ ID NO:51, SEQ ID NO:53, SEQ ID NO:55, SEQ ID NO:57, SEQ ID NO:59, SEQ ID NO:61, SEQ ID NO:63, SEQ ID NO:65, SEQ ID NO:67, SEQ ID NO:69, SEQ ID NO:99, and SEQ ID NO:107.
39. The method of controlling or eradicating an insect population comprising contacting said insect population with an insecticidally-effective amount of a Cry3B* polypeptide composition, wherein:
said composition is substantially free of intact cells, and
said Cry3B* polypeptide in said composition has one or more loop regions between two adjacent α helices and one or more mutations in at least one of said loop regions.
40. The method of claim 39, wherein said polypeptide is selected from the group consisting of Cry3Bb-60, Cry3Bb.11221, Cry3Bb.11222, Cry3Bb.11223, Cry3Bb.11224, Cry3Bb.11225, Cry3Bb.11226, Cry3Bb.11227, Cry3Bb.11228, Cry3Bb.11229, Cry3Bb.11230, Cry3Bb.11231, Cry3Bb.11232, Cry3Bb.11233, Cry3Bb.11234, Cry3Bb.11235, Cry3Bb.11236, Cry3Bb.11237, Cry3Bb.11238, Cry3Bb.11239, Cry3Bb.11241, Cry3Bb.11242, Cry3Bb.11032, Cry3Bb.11035, Cry3Bb.11036, Cry3Bb.11046, Cry3Bb.11048, Cry3Bb.11051, Cry3Bb.11057, Cry3Bb.11058, Cry3Bb.11081, Cry3Bb.11082, Cry3Bb.11083, Cry3Bb.11084, Cry3Bb.11095, and Cry3Bb.11098.
41. The method of claim 39, wherein said Cry3* polypeptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO:2, SEQ ID NO:4, SEQ ID NO:6, SEQ ID NO:8, SEQ ID NO:10, SEQ ID NO:12, SEQ ID NO:14, SEQ ID NO:16, SEQ ID NO:18, SEQ ID NO:20, SEQ ID NO:22, SEQ ID NO:24, SEQ ID NO:26, SEQ ID NO:28, SEQ ID NO:30, SEQ ID NO:32, SEQ ID NO:34, SEQ ID NO:36, SEQ ID NO:38, SEQ ID NO:40, SEQ ID NO:42, SEQ ID NO:44, SEQ ID NO:46, SEQ ID NO:48, SEQ ID NO:50, SEQ ID NO:52, SEQ ID NO:54, SEQ ID NO:56, SEQ ID NO:58, SEQ ID NO:60, SEQ ID NO:62, SEQ ID NO:64, SEQ ID NO:66, SEQ ID NO:68, SEQ ID NO:70, SEQ ID NO:100, and SEQ ID NO:108.
Priority Applications (20)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/993,775 US6077824A (en) | 1997-12-18 | 1997-12-18 | Methods for improving the activity of δ-endotoxins against insect pests |
| PCT/US1998/026852 WO1999031248A1 (en) | 1997-12-18 | 1998-12-17 | INSECT-RESISTANT TRANSGENIC PLANTS AND METHODS FOR IMPROVING δ-ENDOTOXIN ACTIVITY AGAINST TARGET INSECTS |
| ES98964762T ES2273447T3 (en) | 1997-12-18 | 1998-12-17 | INSECT RESISTANT TRANSGEN PLANTS AND PROCEDURES TO IMPROVE INSECT ACTIVITY. |
| DK98964762T DK1040192T3 (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving delta-endotoxin activity against insects |
| BRPI9814294-1A BR9814294B1 (en) | 1997-12-18 | 1998-12-17 | b cry3bb polypeptide, modified thuringiensis, composition comprising the same, process for producing said composition, polynucleotide, vector, virus, transgenic microorganism and methods for killing and controlling a coleopteran insect population and for preparing a transgenic plant resistant to beetles and a Coleoptera-resistant plant seed and a Coleoptera-resistant plant seed. |
| AU20013/99A AU2001399A (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving delta-endotoxin activity against target insects |
| AT06118584T ATE555123T1 (en) | 1997-12-18 | 1998-12-17 | INSECT-RESISTANT TRANSGENIC PLANTS AND METHODS TO IMPROVE DELTA-TOXIN ACTIVITY AGAINST TARGET INSECTS |
| CA002314429A CA2314429C (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving .delta.-endotoxin activity against target insects |
| CNB988137135A CN100340666C (en) | 1997-12-18 | 1998-12-17 | Insect-risistant transgenic plants and methods for improving 'delta' -endotoxin activity against target insects |
| EP06118584A EP1749834B1 (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving delta-endotoxin activity against target insects |
| DE69835538T DE69835538T2 (en) | 1997-12-18 | 1998-12-17 | INSECT-RESISTANT TRANSGENIC PLANTS AND METHOD FOR IMPROVING THE ACTIVITY OF DELTA ENDOTOXINS AGAINST INSECTS |
| EP98964762A EP1040192B1 (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving delta-endotoxin activity against insects |
| PT98964762T PT1040192E (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving delta-endotoxin activity against insects |
| AT06118582T ATE544857T1 (en) | 1997-12-18 | 1998-12-17 | INSECT-RESISTANT TRANSGENIC PLANTS AND METHOD FOR IMPROVING THE ACTIVITY OF DELTA-ENDOTOXINS AGAINST INSECTS |
| AT98964762T ATE335822T1 (en) | 1997-12-18 | 1998-12-17 | INSECT-RESISTANT TRANSGENIC PLANTS AND METHOD FOR IMPROVING THE ACTIVITY OF DELTA-ENDOTOXINS AGAINST INSECTS |
| EP06118582A EP1801220B1 (en) | 1997-12-18 | 1998-12-17 | Insect-resistant transgenic plants and methods for improving delta-endotoxin activity against insects |
| ARP980106508A AR014144A1 (en) | 1997-12-18 | 1998-12-18 | MODIFIED CRY3BB POLYEPTIDE OF B. THURINGIENSIS, INSECTICIATED COMPOSITION, POLINUCLEOTIDE, VECTOR, MODIFIED MICROORGANISM, METHOD FOR KILLING A COLEOPTEROUS INSECT, METHOD FOR PREPARING A SEED OF A PLANT, METHOD FOR CONTROLLING A POBLATION AND A BODY METHOD |
| ARP000101927A AR023762A2 (en) | 1997-12-18 | 2000-04-24 | METHOD FOR PRODUCING A CRY3BB MODIFIED POLYPEPTIDE WITH IMPROVED INSECTICIATED ACTIVITY OR SPECIFICITY, METHOD FOR INCREASING THE CHANNELS OF CHANNELS OF A CRY3BB POLYPEPTIDE, METHOD FOR INCREASING THE FLEXIBILITY OF A BUCLE CAN REGION FORM |
| CY20061101610T CY1106323T1 (en) | 1997-12-18 | 2006-11-08 | TRANSGENIC INSECT-RESISTANT PLANTS AND METHODS OF IMPROVING DELTA-ENDOTOXIN ACTIVITY AGAINST INSECT TARGETS |
| ARP080100051A AR064767A2 (en) | 1997-12-18 | 2008-01-07 | CRY3BB * POLYPEPTIDE MODIFIED BACILLUS THURINGIENSIS COMPOSITION THAT INCLUDES IT, POLINUCLEOTIDE, VECTOR, VIRUS, TRANSFORMED GUY CELL, USE OF THE CRY3BB POLYPEPTIDE *, METHOD TO KILL A COLEOPTEROUS METHOD INSTRUMENT, A METHODOUS CONTROLLING METHOD |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US08/993,775 US6077824A (en) | 1997-12-18 | 1997-12-18 | Methods for improving the activity of δ-endotoxins against insect pests |
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| US6077824A true US6077824A (en) | 2000-06-20 |
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| Application Number | Title | Priority Date | Filing Date |
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| US08/993,775 Expired - Lifetime US6077824A (en) | 1997-12-18 | 1997-12-18 | Methods for improving the activity of δ-endotoxins against insect pests |
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